Crystal structure of dimeric HIV-1 capsid protein
Crystal structure of dimeric HIV-1 capsid protein
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DOI：
10.1038/nsb0996-763
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发表时间：
1996-09-01
期刊：
影响因子：
--
通讯作者：
Rossmann, MG
中科院分区：
文献类型：
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作者：
Momany, C;Kovari, LC;Rossmann, MG
人类免疫缺陷病毒 (HIV-1) 衣壳 (CA) 蛋白的 X 射线衍射分析表明，二聚体中的每个单体均由七个 α 螺旋组成，其中五个螺旋排列成卷曲的螺旋结构。对其中两个螺旋进行了序列分配，并且通过单体 N 末端片段的最新解决方案结构证实了蛋白质其余部分的初步连接。蛋白质的 C 端三分之一在晶体中大部分是无序的。卷曲的螺旋状结构中最长的螺旋被长的、高抗原性的肽分开，该肽包括与晶体中的 CA 复合的抗体片段的结合位点。 Fab 的结合位点、抗原环的位置以及基质蛋白和 CA 之间的切割位点确定了二聚体位于逆转录病毒核心外部的一侧。
X-ray diffraction analysis of a human immunodeficiency virus (HIV-1) capsid (CA) protein shows that each monomer within the dimer consists of seven alpha-helices, five of which are arranged in a coiled coil-like structure. Sequence assignments were made for two of the helices, and tentative connectivity of the remainder of the protein was confirmed by the recent solution structure of a monomeric N-terminal fragment. The C-terminal third of the protein is mostly disordered in the crystal. The longest helices in the coiled coil-like structure are separated by a long, highly antigenic peptide that includes the binding site of an antibody fragment complexed with CA in the crystal. The site of binding of the Fab, the position of the antigenic loop and the site of cleavage between the matrix protein and CA establish the side of the dimer that would be on the exterior of the retroviral core.