Model for the structure of the HIV gp41 ectodomain: insight into the intermolecular interactions of the gp41 loop

被引:65
作者
Caffrey, M [1 ]
机构
[1] Univ Illinois, Dept Biochem & Mol Biol, Chicago, IL 60612 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE | 2001年 / 1536卷 / 2-3期
关键词
AIDS; envelope proteins; gp120; complement;
D O I
10.1016/S0925-4439(01)00042-4
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
In human immunodeficiency virus (HIV) the viral envelope proteins gp41 and gp120 form a non-covalent complex, which is a potential target for AIDS therapies. In addition gp41 plays a possible role in HIV infection of B cells via the complement system. In an effort to better understand the molecular interactions of gp41, the structure of the HIV gp41 ectodomain has been modeled using the NMR restraints of the simian immunodeficiency virus (SIV) gp41 ectodomain (M. Caffrey, M. Cai, J. Kaufman, S.J. Stahl, P.T. Wingfield, A.M. Gronenborn, G.M. Clore, Solution structure of the 44 kDa ectodomain of SIV gp41, EMBO J. 17 (1998) 4572-4584). The resulting model presents the first structural information for the HIV gp41 loop, which has been implicated to play a direct role in binding to gp120 and Clq of the complement system. (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:116 / 122
页数:7
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