Comprehensive mutagenesis of HIV-1 protease: a computational geometry approach

被引：22

作者：

Masso, M ^{[1
]}

Vaisman, II ^{[1
]}

机构：

[1] George Mason Univ, Sch Computat Sci, Manassas, VA 20110 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 305卷 / 02期

关键词：

statistical geometry; Delaunay tessellation; molecular modeling; protein structured; computational mutagenesis; HIV-1; protease;

D O I：

10.1016/S0006-291X(03)00760-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A computational geometry technique based on Delaunay tessellation of protein structure, represented by C-x atoms, is used to study effects of single residue mutations on sequence-structure compatibility in HIV-1 protease. Profiles of residue scores derived from the four-body statistical potential are constructed for all 1881 mutants of the HIV-1 protease monomer and compared with the profile of the wild-type protein. The profiles for an isolated monomer of HIV-1 protease and the identical monomer in a dimeric state with an inhibitor are analyzed to elucidate changes to structural stability. Protease residues shown to undergo the greatest impact are those forming the dimer interface and flap region, as well as those known to be involved in inhibitor binding. (C) 2003 Elsevier Science (USA). All rights reserved.

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页码：322 / 326

页数：5

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