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Information on EC 3.4.23.B2 - Simian immunodeficiency virus proteinase
for references in articles please use BRENDA:EC3.4.23.B2preliminary BRENDA-supplied EC number
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EC Tree
3.4.23.B2 Simian immunodeficiency virus proteinaseSpecify your search results
Word Map
- 3.4.23.B2
- transcriptase
-
integrase
-
retroviral
-
foamy
-
transframe
-
mauritian
- dutpase
-
pol-specific
The expected taxonomic range for this enzyme is: Simian immunodeficiency virus
Reaction Schemes
The enzyme may have a wide substrate specificity. Good cleavage of the peptide bonds Met-Met and Tyr-Pro. Cleavage is also observed at Phe-Pro, Phe-Leu, Leu-Phe, Leu-Ala, Glu-Ala and Tyr-Ala
Synonyms
pol polyprotein, siv protease, retropepsin, siv-pr, siv pr, siv proteinase, simian immunodeficiency virus protease, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Pol polyprotein
-
-
-
-
retropepsin
-
-
-
-
Simian immunodeficiency virus protease
SIV PR
-
-
-
-
SIV protease
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-
-
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SIV proteinase
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-
-
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SIV-PR
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-
-
-
additional information
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the enzyme belongs to the A2 peptidase family
Simian immunodeficiency virus protease
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The enzyme may have a wide substrate specificity. Good cleavage of the peptide bonds Met-Met and Tyr-Pro. Cleavage is also observed at Phe-Pro, Phe-Leu, Leu-Phe, Leu-Ala, Glu-Ala and Tyr-Ala
The enzyme may have a wide substrate specificity. Good cleavage of the peptide bonds Met-Met and Tyr-Pro. Cleavage is also observed at Phe-Pro, Phe-Leu, Leu-Phe, Leu-Ala, Glu-Ala and Tyr-Ala
-
-
-
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The enzyme may have a wide substrate specificity. Good cleavage of the peptide bonds Met-Met and Tyr-Pro. Cleavage is also observed at Phe-Pro, Phe-Leu, Leu-Phe, Leu-Ala, Glu-Ala and Tyr-Ala
aspartic acid protease, structure-function relation ship, the active site conformation changes from open to closed upon substrate binding, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-Ala-Thr-Leu-Asn-Phe-Pro-Ile-Ser-Pro-Ile-Glu-NH2 + H2O
Ac-Ala-Thr-Leu-Asn-Phe + Pro-Ile-Ser-Pro-Ile-Glu-NH2
-
-
-
?
Ac-Arg-Ala-Ser-Gln-Asn-Tyr-Pro-Val-Val-NH2 + H2O
Ac-Arg-Ala-Ser-Gln-Asn-Tyr-OH + Pro-Val-Val-NH2
Ac-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly-NH2 + H2O
Ac-Arg-Lys-Ile-Leu + Phe-Leu-Asp-Gly-NH2
-
-
-
-
?
Ac-Ser-Gln-Asn-Tyr-Pro-Val-Val-NH2 + H2O
Ac-Ser-Gln-Asn-Tyr + Pro-Val-Val-NH2
-
-
-
?
acetyl-Arg-Ala-Ser-Gln-Asn-Tyr-Pro-Val-Val + H2O
acetyl-Arg-Ala-Ser-Gln-Asn-Tyr + Pro-Val-Val
-
-
-
-
?
aminobenzoyl-Thr-Ile-Nle-Phe(p-NO2)-Gln-Arg-NH2 + H2O
?
-
-
-
-
?
biotin-Gly-Gly-Asp-Arg-Gly-Phe-Ala-Ala-Pro-Gln-Phe-Ser-Leu-Trp-Arg-Arg + H2O
biotin-Gly-Gly-Asp-Arg-Gly-Phe-Ala-Ala + Pro-Gln-Phe-Ser-Leu-Trp-Arg-Arg
-
-
-
?
Lys-Ala-Arg-Val-Nle-(NO2)Phe-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Nle + (NO2)Phe-Glu-Ala-Nle-Gly
oxidized insulin B chain + H2O
?
-
cleavage sites: HLVE13-ALYL and EALY16-LVC[SO3-]G
-
-
?
SIV Gag precursor protein + H2O
?
-
determination of cleavage sites and substrate specificity
-
-
?
troponin C + H2O
?
-
cleavage sites: EEEL97-AECF and AEEL117-AEIF
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val
-
-
-
?
additional information
?
-
-
cleavage site in Lys-PE40, a construct based upon the Pseudomonas exotoxin OE66 that is missing domain I are: ANL-1-AEEA and GDAL389-LERN
-
-
?
Ac-Arg-Ala-Ser-Gln-Asn-Tyr-Pro-Val-Val-NH2 + H2O
Ac-Arg-Ala-Ser-Gln-Asn-Tyr-OH + Pro-Val-Val-NH2
-
-
-
?
Ac-Arg-Ala-Ser-Gln-Asn-Tyr-Pro-Val-Val-NH2 + H2O
Ac-Arg-Ala-Ser-Gln-Asn-Tyr-OH + Pro-Val-Val-NH2
-
-
-
-
?
galactokinase + H2O
?
-
galactokinase engineered with individual cleavage sites. Cleaves the sites in the order of decreasing preference: Met-Met, Phe-Pro, Leu-Phe, Tyr-Pro, Phe-Leu, Leu-Ala
-
-
?
galactokinase + H2O
?
-
galactokinase engineered with individual cleavage sites. Cleaves the sites in the order of decreasing preference: Met-Met, Phe-Pro, Leu-Phe, Tyr-Pro, Phe-Leu, Leu-Ala
-
-
?
Lys-Ala-Arg-Val-Nle-(NO2)Phe-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Nle + (NO2)Phe-Glu-Ala-Nle-Gly
-
-
-
?
Lys-Ala-Arg-Val-Nle-(NO2)Phe-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Nle + (NO2)Phe-Glu-Ala-Nle-Gly
-
-
-
?
Lys-Ala-Arg-Val-Nle-(NO2)Phe-Glu-Ala-Nle-Gly + H2O
Lys-Ala-Arg-Val-Nle + (NO2)Phe-Glu-Ala-Nle-Gly
-
-
-
?
Pr55Gag polyprotein + H2O
?
-
lentiviral Gag polyprotein, proteolytic processing for activation, cleavage in the late stages of life cycle, required for maturation of the virion meaning a structural rearrangement required for infectivity in budding virions, cleavage in the phosphorylated capsid domains, the enzyme is not influenced by the preceeding phosphorylation, but cleaved sites are no longer phosphorylated, while incompletely cleaved capsid domains are phosphorylated to a greater extent, overview
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-
?
Pr55Gag polyprotein + H2O
?
-
lentiviral Gag polyprotein, cleavage in the phosphorylated capsid domains, the enzyme is not influenced by the preceeding phosphorylation, but cleaved sites are no longer phosphorylated, while incompletely cleaved capsid domains are phosphorylated to a greater extent, overview
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-
?
Pr55Gag polyprotein + H2O
?
-
PR cleaves Pr55Gag into its constituent domains: matrix (MA), capsid (CA), nucleocapsid (NC), and p6
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Pr55Gag polyprotein + H2O
?
-
lentiviral Gag polyprotein, proteolytic processing for activation, cleavage in the late stages of life cycle, required for maturation of the virion meaning a structural rearrangement required for infectivity in budding virions, cleavage in the phosphorylated capsid domains, the enzyme is not influenced by the preceeding phosphorylation, but cleaved sites are no longer phosphorylated, while incompletely cleaved capsid domains are phosphorylated to a greater extent, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
-
1 M NaCl, rate of substrate cleavage increases up to 4fold
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-naphthoxyacetyl-His-cyclohexylacetyl-PSI[CH(OH)CH(OH)]Val-Ile-2-pyridylmethylamine
-
-
9H-fluoren-9-ylmethyl 7-oxa-3-azabicyclo[4.1.0]heptane-3-carboxylate
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specific irreversible inhibition, t1/2 for inactivation is 240 min with a 0.1 mM inhibitor concentration
phenoxyacetyl-His-cyclohexylacetyl-PSI[CH(OH)CH(OH)]Phe-Ile-2-pyridylmethylamine
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phenoxyacetyl-His-Leu-PSI[CH(OH)CH2]Phe-Ile-2-pyridylmethylamine
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1,2-epoxy-3-(4-nitrophenoxy)propane
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i.e. EPNP; irreversible inactivation, half-maximal inactivation at 8.6 mM
1,2-epoxy-3-(4-nitrophenoxy)propane
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half-maximal inactivation rate at 8.04 mM; i.e. EPNP
additional information
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development of a more efficient irreversible inhibitor can be achieved by optimizing the interactions of the inhibitor with the protein while preserving the favorable reactivity and orientation of the epoxide moiety
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additional information
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fusion of HIV-2-Vpx with an enzymatically defective proteases mutant, PR. The Vpx-PR-mutant fusion protein, Vpx-PRM is expressed and packaged efficiently into simian immunodeficiency virus. VpxPRM specifically inhibits the function of the viral protease
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additional information
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to design inhibitors that are equally effective against HIV-1 and HIV-2, one must maintain a balance in the size of the side chains at P2, P1, P1', and P2'
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additional information
-
several HIV-1 peptomimetic inhibitors also inhibit the SIV retropepsin, inhibitor binding structure
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additional information
-
not inhibitory: HIV-protease inhibitors nelfinavir, saquinavir, darunavir
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
High-resolution structure of a retroviral protease folded as a monomer.
Acquired Immunodeficiency Syndrome
Purification and biochemical characterization of recombinant simian immunodeficiency virus protease and comparison to human immunodeficiency virus type 1 protease.
Infections
Development of [Ile??]HTLV-I protease inhibition assay using novel fluorogenic and chromogenic substrate.
Infections
Purification and biochemical characterization of recombinant simian immunodeficiency virus protease and comparison to human immunodeficiency virus type 1 protease.
Leukemia
Human endogenous retroviruslike genome with type C pol sequences and gag sequences related to human T-cell lymphotropic viruses.
Rickettsia Infections
RC1339/APRc from Rickettsia conorii is a novel aspartic protease with properties of retropepsin-like enzymes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.6
Ac-Ala-Thr-Leu-Asn-Phe-Pro-Ile-Ser-Pro-Ile-Glu-NH2
-
pH 6, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
Ac-Ala-Thr-Leu-Asn-Phe-Pro-Ile-Ser-Pro-Ile-Glu-NH2
-
pH 6, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
1-naphthoxyacetyl-His-cyclohexylacetyl-PSI[CH(OH)CH(OH)]Val-Ile-2-pyridylmethylamine
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pH 5.5, 30°C
0.2
Ac-cyclohexylacetyl-PSI[CH(OH)CH2]Val-Glu-Arg-NH2
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pH 5.5, 30°C
0.000012
Ala-Ala-Phe-Psi[CH(OH)CH2]Gly-Val-ValOCH3
-
pH 4.7, 37°C
0.006
H-Val-Ser-Gln-Asn-Leu-PSI[CH(OH)CH2]Val-Ile-Val-OH
-
pH 5.5, 30°C
0.49
phenoxyacetyl-His-cyclohexylacetyl-PSI[CH(OH)CH(OH)]Phe-Ile-2-pyridylmethylamine
-
pH 5.5, 30°C
0.19
phenoxyacetyl-His-Leu-PSI[CH(OH)CH2]Phe-Ile-2-pyridylmethylamine
-
pH 5.5, 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
Ac-Ser-Gln-Asn-Tyr-Pro-Val-Val-NH2 or Ac-Arg-Lys-Ile-Leu-Phe-Leu-Asp-Gly as substrate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: 60% of maximal activity, 50°C: about 80% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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brenda
SIV, a lenti-retrovirus, derived from different monkey species, the virus is pathogenic not in all of the species, overview
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brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). POL_SIVVT
Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1)
1467
0
166058
Swiss-Prot
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
the active enzyme is a homodimer, each subunit contains an Asn-Thr-Gly aspartic acid protease motif
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the retropepsin is expressed as part of a larger polyprotein precursor, which it cleaves into functional proteins, the major autodegradation site of the enzyme is Phe3-Ser4
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of the enzyme bound to the inhibitor SKF107457, hanging drop method of vapor diffusion
-
crystal structure determination and analysis of free enzyme and enzyme-inhibitor complexes, e.g. with 1,2-epoxy-3-(4-nitrophenoxy)propane at 2.4 A resolution, or with SKF107457 at 2.5 A resolution
-
enzyme covalently bound to the inhibitor 1,2-epoxy-3-(p-nitrophenoxy)propane. Crystals of the variant SIV PR S4H appear to have the same morphology as those obtained from wild-type enzyme
-
hanging-drop crystallization of the K69H mutant enzyme with pepstatin A
-
SIV protease product complex, hanging drop vapor diffusion method
-
unliganded SIV protease crystals are grown by hanging drop vapor diffusion. Domain flexibility and structural implications for drug resistant mutations
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D25N
-
totally inactive mutant enzyme, incapable of autoprocessing
K69H
-
the isoelectric point of the mutant enzyme is pH 7.0 compared to that of the wild-type enzyme of 7.4. The purified mutant enzyme is less soluble at low pH when concentrating sample in preparation for crystallization
S4H
additional information
S4H
-
mutation does not significantly affect the kinetic parameters of the enzyme but stabilizes it approximately 4fold to autolysis. Crystals of the variant SIV PR S4H appear to have the same morphology as those obtained from wild-type enzyme
S4H
-
site-directed mutagenesis, the mutation of the major autodegeneration site stabilizes the enzyme without significantly affecting the kinetic parameters
additional information
-
generation of an protease-inactive mutant of SIVmac239, the phosphorylation pattern of the mutant Pr55Gag protein is unaltered compared to the wild-type, overview
additional information
-
it is demonstrated that the SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag by viral protease
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
-
activity is slightly diminished, less than 30%, after preincubation at pH 7.0-8.0
647815
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 50 mM sodium acetate, pH 5.0, 5 mM EDTA, 10 mM DTT, 0.35 NaCl, 40% v/v glycerol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by ammonium sulfate fractionation, and ion exchange or affinity chromatography on a pepstatin A resin, recombinant N-terminally capped, biotin-labeled precursor by streptavidin affinity chromatography, the tag is autocatalytically cleaved after refolding of the enzyme
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned directly from proviral DNA of the infectious viral stock SIVmac251-32H(11/88 pool). SIVmac251-32H proteinase and ist flanking pol sequences are expressed in Escherichia coli as a fusion protein with most of the T7 bacteriophage gene 10 protein. The expressed protein forms cytoplasmic inclusion bodies which are solubilized in 8 M urea, and the recombinant enzyme is refolded, yielding active self-processing enzyme
-
expressed in Escherichia coli with a recombinant expression system
-
expression in Escherichia coli, expression as N-terminally capped, biotin-labeled precursor
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
nearly total restoration of protein fluorescence upon cooling to 25°C of the enzyme which has been unfolded at 70°C
-
refolding from recombinant cytoplasmic inclusion bodies, refolding of recombinant N-terminally capped, biotin-labeled precursor
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
SIV retropepsin can serve as an inhibitor-resistant retrovirus variant model of HIV-1 retropepsin
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fukasawa, M.; Miura, T.; Hasegawa, A.; Mirikawa, S.; Tsujimoto, H.; Miki, K.; Kitamura, T.; Hayami, M.
Sequence of simian immunodeficiency virus from African green monkey, a new member of HIV/SIV group
Nature
33
457-461
1988
Simian immunodeficiency virus (P05895)
-
brenda
Wilderspin, A.F.; Sugrue, R.J.
Crystallization and preliminary X-ray investigation of recombinant simian immunodeficiency virus proteinase
J. Mol. Biol.
231
1139-1142
1993
Simian immunodeficiency virus, Simian immunodeficiency virus mac251-32H
brenda
Corr, B.R.; Wilderspin, A.F.
Crystallization and biochemical characterisation of simian immunodeficiency virus proteinase mutant
Biochem. Soc. Trans.
22
55S
1994
Simian immunodeficiency virus
brenda
Debouck, C.
Substrate specificity of the human (type 1) and simian immunodeficiency virus proteases
Adv. Exp. Med. Biol.
306
407-415
1991
Simian immunodeficiency virus, Simian immunodeficiency virus MAC
brenda
Sugrue, R.J.; Almond, N.; Kitchin, P.; Richardson, S.M.; Wilderspin, A.F.
Purification of crystallizable recombinant SIVmac251-32H proteinase
Protein Expr. Purif.
5
76-83
1994
Simian immunodeficiency virus, Simian immunodeficiency virus mac251-32H
brenda
Black, P.L.; Downs, M.B.; Lewis, M.G.; Ussery, M.A.; Dreyer, G.B.; Petteway, S.R., Jr.; Lambert, D.M.
Antiretroviral activities of protease inhibitors against murine leukemia virus and simian immunodeficiency virus in tissue culture
Antimicrob. Agents Chemother.
37
71-77
1993
Simian immunodeficiency virus
brenda
Bechtold, C.M.; Patrick, A.K.; Alam, M.; Greytok, J.; Tino, J.A.; Chen, P.; Gordon, E.; Ahmad, S.; Barrish, J.C.; et al.
Antiviral properties of aminodiol inhibitors against Human immunodeficiency virus and protease
Antimicrob. Agents Chemother.
39
374-379
1995
Simian immunodeficiency virus, Simian immunodeficiency virus mac251
brenda
Tomasselli, A.G.; Bannow, C.A.; Deibel, M.R., Jr.; Hui, J.O.; Zurcher-Neely, H.A.; Reardon, I.M.; Smith, C.W.; Heinrikson, R.L.
Chemical synthesis of a biotinylated derivative of the simian immunodeficiency virus protease. Purification by avidin affinity chromatography and autocatalytic activation
J. Biol. Chem.
267
10232-10237
1992
Simian immunodeficiency virus
brenda
Caldera, P.S.; Yu, Z.; Knegtel, R.M.; McPhee, F.; Burlingame, A.L.; Craik, C.S.; Kuntz, I.D.; Ortiz de Montellano, P.R.
Alkylation of a catalytic aspartate group of the SIV protease by an epoxide inhibitor
Bioorg. Med. Chem.
5
2019-2027
1997
Simian immunodeficiency virus
brenda
Wu, X.; Liu, H.; Xiao, H.; Conway, J.A.; Kappes, J.C.
Inhibition of human and simian immunodeficiency virus protease function by targeting Vpx-protease-mutant fusion protein into viral particles
J. Virol.
70
3378-3384
1996
Simian immunodeficiency virus
brenda
Rose, R.B.; Craik, C.S.; Stroud, R.M.
Domain flexibility in retroviral proteases: Structural implications for drug resistant mutations
Biochemistry
37
2607-2621
1998
Simian immunodeficiency virus
brenda
Grant, S.K.; Deckman, I.C.; Minnich, M.D.; Culp, J.; Franklin, S.; Dreyer, G.B.; Tomaszek, T.A., Jr.; Debouck, C.; Meek, T.D.
Purification and biochemical characterization of recombinant simian immunodeficiency virus protease and comparison to human immunodeficiency virus type 1 protease
Biochemistry
30
8424-8434
1991
Simian immunodeficiency virus
brenda
Grant, S.K.; Deckman, I.C.; Culp, J.S.; Minnich, M.D.; Brooks, I.S.; Hensley, P.; Debouck, C.; Meek, T.D.
Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases
Biochemistry
31
9491-9501
1992
Simian immunodeficiency virus
brenda
Zhao, B.; Winborne, E.; Minnich, M.D.; Culp, J.S.; Debouck, C.; Abdel-Meguid, S.S.
Three-dimensional structure of a simian immunodeficiency virus protease/inhibitor complex. Implications for the design of human immunodeficiency virus type 1 and 2 protease inhibitors
Biochemistry
32
13054-13060
1993
Simian immunodeficiency virus
brenda
Rose, R.B.; Craik, C.S.; Douglas, N.L.; Stroud, R.M.
Three-dimensional structures of HIV-1 and SIV protease product complexes
Biochemistry
35
12933-12944
1996
Simian immunodeficiency virus
brenda
Rose, R.B.; Rose, J.R.; Salto, R.; Craik, C.S.; Stroud, R.M.
Structure of the protease from simian immunodeficiency virus: complex with an irreversible nonpeptide inhibitor
Biochemistry
32
12498-12507
1993
Simian immunodeficiency virus
brenda
Konvalinka, J.; Kraeusslich, H.
Simian immunodeficiency virus retropepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
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Simian immunodeficiency virus
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Rue, S.M.; Roos, J.W.; Tarwater, P.M.; Clements, J.E.; Barber, S.A.
Phosphorylation and proteolytic cleavage of Gag proteins in budded simian immunodeficiency virus
J. Virol.
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2005
Simian immunodeficiency virus
brenda
Nicholson, M.G.; Barber, S.A.; Clements, J.E.
The SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag
Virology
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84-91
2007
Simian immunodeficiency virus
brenda
Togami, H.; Shimura, K.; Okamoto, M.; Yoshikawa, R.; Miyazawa, T.; Matsuoka, M.
Comprehensive in vitro analysis of simian retrovirus type 4 susceptibility to antiretroviral agents
J. Virol.
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Simian immunodeficiency virus
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