Analysis of the full-length integrase - DNA complex by a modified approach for DNA docking

被引：55

作者：

De Luca, L

Pedretti, A

Vistoli, G

Barreca, ML

Villa, L

Monforte, P

Chimirri, A

机构：

[1] Univ Messina, Dipartimento Farmacochim, I-98168 Messina, Italy

[2] Univ Milan, Fac Farm, Inst Chim Farmaceut, I-20131 Milan, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 310卷 / 04期

关键词：

HIV-1; integrase; DNA-protein docking; full-length IN-DNA complex;

D O I：

10.1016/j.bbrc.2003.09.120

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 model of the full-length HIV-1 integrase dimer was constructed assembling the experimentally determined structures of the single domains. Subsequently, the three-domain protein-viral DNA complex was generated for the first time through an automated docking algorithm, obtained modifying the ESCHER program, a well-known method for protein-protein docking. A detailed study of the contacts established with DNA by the enzyme revealed that the predicted model reproduced the results of mutagenesis and cross-linking experiments, confirming the validity of our docking approach in predicting the base specificity in the DNA-protein interaction. (C) 2003 Elsevier Inc. All rights reserved.

引用

页码：1083 / 1088

页数：6

共 45 条

[1]

*ACC INC, 2001, INS

[2]

Ausiello G, 1997, PROTEINS, V28, P556, DOI 10.1002/(SICI)1097-0134(199708)28:4<556::AID-PROT9>3.3.CO

[3]

2-C

[4] CHARMM - A PROGRAM FOR MACROMOLECULAR ENERGY, MINIMIZATION, AND DYNAMICS CALCULATIONS [J].