Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein

被引：514

作者：

Gamble, TR ^{[1
]}

Yoo, SH ^{[1
]}

Vajdos, FF ^{[1
]}

vonSchwedler, UK ^{[1
]}

Worthylake, DK ^{[1
]}

Wang, H ^{[1
]}

McCutcheon, JP ^{[1
]}

Sundquist, WI ^{[1
]}

Hill, CP ^{[1
]}

机构：

[1] UNIV UTAH,DEPT BIOCHEM,SALT LAKE CITY,UT 84132

来源：

SCIENCE | 1997年 / 278卷 / 5339期

关键词：

D O I：

10.1126/science.278.5339.849

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The carboxyl-terminal domain, residues 146 to 231, of the human immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required for capsid dimerization and viral assembly. This domain contains a stretch of 20 residues, called the major homology region (MHR), which is conserved across retroviruses and is essential for viral assembly, maturation, and infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal that the globular domain is composed of four helices and an extended aminoterminal strand. CA(146-231) dimerizes through parallel packing of helix 2 across a dyad. The MHR is distinct from the dimer interface and instead forms an intricate hydrogen-bonding network that interconnects strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.

引用

页码：849 / 853

页数：5

共 36 条

[11] Structure of the amino-terminal core domain of the HIV-1 capsid protein [J].