15gag proteinase of myeloblastosis-associated virus: specificity studies with substrate-based inhibitors
Language English Country United States Media print
Document type Comparative Study, Journal Article
PubMed
1417001
DOI
10.1016/0003-9861(92)90476-d
PII: 0003-9861(92)90476-D
Knihovny.cz E-resources
- MeSH
- Aspartic Acid Endopeptidases antagonists & inhibitors MeSH
- HIV-1 enzymology MeSH
- HIV Protease metabolism MeSH
- Protease Inhibitors chemical synthesis pharmacology MeSH
- Kinetics MeSH
- Molecular Sequence Data MeSH
- Oligopeptides chemical synthesis pharmacology MeSH
- Amino Acid Sequence MeSH
- Substrate Specificity MeSH
- Avian Myeloblastosis Virus enzymology MeSH
- Structure-Activity Relationship MeSH
- Publication type
- Journal Article MeSH
- Comparative Study MeSH
- Names of Substances
- Aspartic Acid Endopeptidases MeSH
- HIV Protease MeSH
- Protease Inhibitors MeSH
- Oligopeptides MeSH
- protease p15 MeSH Browser
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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