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
Autori: | |
Data di pubblicazione: | 2001 |
Titolo: | Allosteric Regulation of a HIV-1 Protease Inhibitor by Zn(II) Ions |
Rivista: | ANGEWANDTE CHEMIE. INTERNATIONAL EDITION |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1002/1521-3773(20011015)40:20<3899::AID-ANIE3899>3.0.CO;2-C |
Volume: | 20 |
Appare nelle tipologie: | 2.1 Articolo su rivista |
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