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15gag proteinase of myeloblastosis-associated virus: specificity studies with substrate-based inhibitors

L Pavlickova, D Stys, M Soucek, J Urban, O Hruskova, J Sedlacek, P Strop

. 1992 ; 298 (2) : 753-756.

Language English Country United States

Document type Comparative Study

Persistent link   https://www.medvik.cz/link/bmc13027641

Grant support
PL19 MZ0 CEP Register

The specificity of the proteinase of myeloblastosis-associated virus (MAV) was studied with (a) 21 substrate-based inhibitors, (b) 9 inhibitors with pseudopalindrome sequences, (c) 8 chimeric inhibitors, and (d) 3 compounds designed as human immunodeficiency virus 1 (HIV-1) proteinase inhibitors. The central inhibitory unit (transition state or cleaved bond analog) and the role of the inhibitor side chains from P4 to P4' were investigated. MAV proteinase prefers an aromatic side chain in P1 and a small aliphatic nonpolar chain in P2 and P2'. Residues in P5 and P4 positions are outside of the short catalytic cleft of the enzyme, but still influence binding considerably. The data obtained provide evidence that the MAV proteinase has generally lower specificity and poorer binding than the HIV proteinase.

Bibliography, etc.

Literatura

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$a The specificity of the proteinase of myeloblastosis-associated virus (MAV) was studied with (a) 21 substrate-based inhibitors, (b) 9 inhibitors with pseudopalindrome sequences, (c) 8 chimeric inhibitors, and (d) 3 compounds designed as human immunodeficiency virus 1 (HIV-1) proteinase inhibitors. The central inhibitory unit (transition state or cleaved bond analog) and the role of the inhibitor side chains from P4 to P4' were investigated. MAV proteinase prefers an aromatic side chain in P1 and a small aliphatic nonpolar chain in P2 and P2'. Residues in P5 and P4 positions are outside of the short catalytic cleft of the enzyme, but still influence binding considerably. The data obtained provide evidence that the MAV proteinase has generally lower specificity and poorer binding than the HIV proteinase.
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$a Souček, Milan, $d 1930- $7 jk01120477 $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
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$a Hrušková-Heidingsfeldová, Olga $7 xx0060514 $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
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