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Literature summary for 3.4.23.B8 extracted from

  • Kheirabadi, M.; Maleki, J.; Soufian, S.; Hosseini, S.
    Design of new potent HTLV-1 protease inhibitors in silico study (2016), Mol. Biol. Res. Commun., 5, 19-30 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.B8

Inhibitors

Inhibitors Comment Organism Structure
(2R)-2-[(3-[[(R)-amino(hydroxy)methyl][2-hydroxy-2-(naphthalen-2-yl)ethyl]amino]-3-cyclopentylpropyl)amino]-N-benzyl-2-hydroxyethanesulfonamide
-
 Human T-cell leukemia virus type I
2-(4-tert-butylphenyl)-N-carbamoyl-N-[3-([[(pyridin-1(2H)-ylmethyl)sulfamoyl]carbonyl]amino)-3-(pyrrolidin-1-yl)propyl]acetamide
-
 Human T-cell leukemia virus type I
2-(4-tert-butylphenyl)-N-carbamoyl-N-[3-[([[(3,5-dichloro-4-oxopyridin-1(4H)-yl)methyl]sulfamoyl]carbonyl)amino]-3-[3-(hydroxyamino)-4-oxopyrrolidin-1-yl]propyl]acetamide strong inhibition, enzyme-bound structure modelling and molecular dynamics Human T-cell leukemia virus type I
KNI-10673
-
 Human T-cell leukemia virus type I
KNI-10681
-
 Human T-cell leukemia virus type I
KNI-10683
-
 Human T-cell leukemia virus type I
KNI-10729
-
 Human T-cell leukemia virus type I
KNI-1595b
-
 Human T-cell leukemia virus type I
KNI1595b
-
 Human T-cell leukemia virus type I
additional information inhibitor design and evaluation of 15 inhibitory compounds based on the conformations of a class of HIV-1 aspartyl protease inhibitor sulfonamid-peptoid, molecular docking study and molecular dynamics simulations, hydrogen bond patterns, overview. The addition of two cyclic hydrocarbons to both ends of sulfonamide peptoids leads to the formation of new hydrophobic interactions due to the semi-circular form of these compounds, connecting the first chain of protease to the two ends of tested ligands via hydrophobic interactions. The strongest H-bond interaction has occurs between 2-(4-tert-butylphenyl)-N-carbamoyl-N-[3-[([[(3,5-dichloro-4-oxopyridin-1(4H)-yl)methyl]sulfamoyl]carbonyl)amino]-3-[3-(hydroxyamino)-4-oxopyrrolidin-1-yl]propyl]acetamide and N-(3-[[(benzylsulfamoyl)carbonyl]amino]-1-cyclopentylpropyl)-N-carbamoyl-N2-hydroxy-N2-(hydroxymethyl)glycinamide inhibitors with both S3 and S4 subsite in first chain of HTLV-1 protease Human T-cell leukemia virus type I
N-(3-[[(benzylsulfamoyl)carbonyl]amino]-1-cyclopentylpropyl)-N-carbamoyl-N2-hydroxy-N2-(hydroxymethyl)glycinamide strong inhibition, enzyme-bound structure modelling and molecular dynamics Human T-cell leukemia virus type I
phenyl (9S)-5-cyclopentyl-3,6,9-trihydroxy-2-(naphthalen-2-yl)-2,5,8,10-tetraazadodecane-12-sulfonate
-
 Human T-cell leukemia virus type I

Organism

Organism UniProt Comment Textmining
Human T-cell leukemia virus type I
-
 HTLV-1
-

Subunits

Subunits Comment Organism
homodimer
-
 Human T-cell leukemia virus type I

Synonyms

Synonyms Comment Organism
HTLV-1 protease
-
 Human T-cell leukemia virus type I

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00000123
-
 N-(3-[[(benzylsulfamoyl)carbonyl]amino]-1-cyclopentylpropyl)-N-carbamoyl-N2-hydroxy-N2-(hydroxymethyl)glycinamide pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.0000219
-
 KNI1595b pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.0000477
-
 2-(4-tert-butylphenyl)-N-carbamoyl-N-[3-[([[(3,5-dichloro-4-oxopyridin-1(4H)-yl)methyl]sulfamoyl]carbonyl)amino]-3-[3-(hydroxyamino)-4-oxopyrrolidin-1-yl]propyl]acetamide pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.000202
-
 2-(4-tert-butylphenyl)-N-carbamoyl-N-[3-([[(pyridin-1(2H)-ylmethyl)sulfamoyl]carbonyl]amino)-3-(pyrrolidin-1-yl)propyl]acetamide pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.000268
-
 phenyl (9S)-5-cyclopentyl-3,6,9-trihydroxy-2-(naphthalen-2-yl)-2,5,8,10-tetraazadodecane-12-sulfonate pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.000306
-
 (2R)-2-[(3-[[(R)-amino(hydroxy)methyl][2-hydroxy-2-(naphthalen-2-yl)ethyl]amino]-3-cyclopentylpropyl)amino]-N-benzyl-2-hydroxyethanesulfonamide pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.00111
-
 KNI-10673 pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.00162
-
 KNI-10729 pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.00197
-
 KNI-10683 pH and temperature not specified in the publication Human T-cell leukemia virus type I
0.00317
-
 KNI-10681 pH and temperature not specified in the publication Human T-cell leukemia virus type I

General Information

General Information Comment Organism
malfunction hydrophobic force plays an important role in suppressing protease activity especially for HTLV-1 protease, which in turn prevents the virus maturity Human T-cell leukemia virus type I
additional information two acidic residues are located in the narrow tunnel-shaped active site of enzyme accommodating substrates or inhibitors. The residues located in the HTLV-1 active site include Arg10, Lys95, Asn96, and Asn97 in the S3 subsite, residues Asp36, Met37, Asn53, Thr54, Ser55, Cys90, and Val92 in the S4 subsite, and residues Leu30, Gly34, Val56, Leu57, Gln96, Gln97, Trp98 in the S1 subsite, as well as two catalytic aspartyl residues (Asp32) positioned in both symmetrical chains of protease Human T-cell leukemia virus type I
physiological function HTLV-1 protease is an aspartic protease responsible for the processing of Gag and Gag-pro-pol polyprotein during virus maturation and catalyzes an essential step in virus replication cycle Human T-cell leukemia virus type I