A sevenfold increase in the ability to bind to the dimerization interface of HIV-1 protease is observed by adding a ZnII 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
Allosteric Regulation of a HIV-1 Protease Inhibitor by Zn(II) Ions
SCARSO, Alessandro;
2001
Abstract
A sevenfold increase in the ability to bind to the dimerization interface of HIV-1 protease is observed by adding a ZnII 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
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