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Allosteric Regulation of an HIV‐1 Protease Inhibitor by Zn II Ions
Author(s) -
Valente Simone,
Gobbo Marina,
Licini Giulia,
Scarso Alessandro,
Scrimin Paolo
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20011015)40:20<3899::aid-anie3899>3.0.co;2-c
Subject(s) - allosteric regulation , monomer , chemistry , hiv 1 protease , protease , enzyme , amine gas treating , stereochemistry , tris , protease inhibitor (pharmacology) , human immunodeficiency virus (hiv) , biochemistry , biology , virology , polymer , organic chemistry , antiretroviral therapy , viral load
A sevenfold increase in the ability to bind to the dimerization interface of HIV‐1 protease is observed by adding a Zn II ion to a tris(aminoethyl)amine (TREN) templating unit, which bears two peptides with similar sequences as those at the C and N termini of each monomer of the dimeric enzyme (see picture). It is suggested that the metal ion changes the conformation of the putative inhibitor.