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M9630545.TXT
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1996-02-27
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Document 0545
DOCN M9630545
TI Mutational analysis of the substrate binding pocket of murine leukemia
virus protease and comparison with human immunodeficiency virus
proteases.
DT 9603
AU Menendez-Arias L; Weber IT; Oroszlan S; Centro de Biologia Molecular
Severo Ochoa, Consejo Superior de; Investigaciones
Cientificas-Universidad Autonoma de Madrid,; Spain.
SO J Biol Chem. 1995 Dec 8;270(49):29162-8. Unique Identifier : AIDSLINE
MED/96094303
AB The differences in substrate specificity between Moloney murine leukemia
virus protease (MuLV PR) and human immunodeficiency virus (HIV) PR were
investigated by site-directed mutagenesis. Various amino acids, which
are predicted to form the substrate binding site of MuLV PR, were
replaced by the equivalent ones in HIV-1 and HIV-2 PRs. The expressed
mutants were assayed with the substrate Val-Ser-Gln-Asn-Tyr decreases
Pro-Ile-Val-Gln-NH2 (decreases indicates the cleavage site) and a series
of analogs containing single amino acid substitutions in positions
P4(Ser) to P3'(Val). Mutations at the predicted S2/S2' subsites of MuLV
PR have a strong influence on the substrate specificity of this enzyme,
as observed with mutants H37D, V39I, V54I, A57I, and L92I. On the other
hand, substitutions at the flap region of MuLV PR often rendered enzymes
with low activity (e.g. W53I/Q55G). Three amino acids (His-37, Val-39,
and Ala-57) were identified as the major determinants of the differences
in substrate specificity between MuLV and HIV PRs.
DE Amino Acid Sequence Base Sequence Binding Sites Comparative Study
HIV Protease/*CHEMISTRY/METABOLISM Leukemia Viruses, Murine/*ENZYMOLOGY
Molecular Sequence Data Mutagenesis, Site-Directed Peptide
Peptidohydrolases/*CHEMISTRY Structure-Activity Relationship Substrate
Specificity Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Viral
Proteins/*CHEMISTRY JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).