3.4.23.B10: Rous sarcoma virus retropepsin

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For detailed information about Rous sarcoma virus retropepsin, go to the full flat file.

Reaction

The cleavage sequence in the natural substrate NC-PR is PPAVS-/-LAMTMRR. The activity can be improved by substitution by Trp, Tyr, Phe, Leu, Arg, Glu, His or Ala in P1, Tyr in P3', and Arg, Phe, Asn or His in P3 =

Synonyms

AMV PR, AMV/RSV PR, avian myeloblastosis virus protease, avian myeloblastosis virus retropepsin, capsid protein P27, core protein P10, core protein P19, core protein P2A, core protein P2B, Gag polyprotein, Gag polyprotein p10 sequence, inner coat protein P12, More, p10-CA protease, p10-capsid protease, p15 protein, protease P15, Rous sarcoma virus protease, Rous sarcoma virus retropepsin, RSV PR, RSV protease, RSV/AMV retropepsin, viral protease

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.B10 Rous sarcoma virus retropepsin

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Results	in table
1	Activating Compound
2	AA Sequence
2	Application
1	CAS Registry Number
6	Cloned(Commentary)
5	Crystallization (Commentary)
2	General Information
2	Inhibitors
2	Ki Value [mM]
28	KM Value [mM]
1	Localization
5	Metals/Ions
2	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
42	Organism
4	pH Optimum
1	pH Range
3	Posttranslational Modification
48	Protein Variants
5	Purification (Commentary)
4	Reaction
1	Reaction Type
29	Reference
1	Renatured (Commentary)
3	Source Tissue
90	Substrates and Products (Substrate)
7	Subunits
29	Synonyms
42	Turnover Number [1/s]

General Information

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General Information on EC 3.4.23.B10 - Rous sarcoma virus retropepsin

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

Rous sarcoma virus

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proteolytic cleavage of Gag by the viral protease (PR) is required for maturation of retroviruses from an immature form into an infectious form. Gag is cleaved by the viral protease enzyme into separate domains, leading to rearrangement of the virus into its infectious form

754541

additional information

Rous sarcoma virus

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the C-terminal domain of RSV conserved capsid (CA) is arranged similarly to HIV-1 and M-PMV, whereas the N-terminal domain of CA adopts a novel arrangement in which the upstream p10 domain folds back into the CA lattice. In this position the cleavage site between CA and p10 appears to be inaccessible to the protease. Below CA, an extended density is consistent with the presence of a six-helix bundle formed by the spacer-peptide region. The cleavage between p10 and CA is indeed inhibited in the assembled lattice, a finding consistent with structural regulation of proteolytic maturation. Docking study and molecular dynamics flexible fitting. The major interaction across the dimeric interface occurs between adjacent hexamers at the CA-CTD is in the region of hydrophobic residues Pro426 and Val427 in helix 9. RSV has a cysteine residue (Cys431) at the base of helix 9 that has been speculated to participate in the interaction across the CA-CTD dimer interface. Modelling shows that the distance between Cys431 residues across the dimer interface is too large to permit disulfide bridge formation in the immature particle

754541