Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
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DOI：
10.1126/science.278.5339.849
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发表时间：
1997-10-31
期刊：
影响因子：
56.9
通讯作者：
Hill, CP
中科院分区：
文献类型：
--
作者：
Gamble, TR;Yoo, SH;Hill, CP
人类免疫缺陷病毒-1（HIV-1）衣壳蛋白[CA（146- 231）]的羧基末端结构域（残基146 - 231）是衣壳二聚化和病毒组装所必需的。该结构域包含一段20个残基，称为主要同源区（MHR），其在逆转录病毒中是保守的，并且对于病毒组装、成熟和感染性是必需的。CA（146-231）和CA（151-231）的晶体结构表明，球状结构域由四个螺旋和一个延伸的氨基末端链组成。CA（146-231）通过螺旋2在二联体中的平行堆积而二聚化。MHR与二聚体界面不同，而是形成一个错综复杂的氢键网络，将链1与螺旋1和2相互连接。CA（146-231）二聚体与衣壳氨基末端结构域的晶体结构的对齐提供了完整蛋白的模型，并扩展了HIV-1中央锥形核心组装的模型。
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.