X-ray crystallographic structure of the Norwalk virus capsid
X-ray crystallographic structure of the Norwalk virus capsid
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DOI：
10.1126/science.286.5438.287
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发表时间：
1999-10-08
期刊：
影响因子：
56.9
通讯作者：
Estes, MK
中科院分区：
文献类型：
--
作者：
Prasad, BVV;Hardy, ME;Estes, MK
Norwalk病毒是一种不可培养的人蜡膜病毒，是人类流行病胃炎的主要原因。蜡膜圈的第一个X射线结构由180个单个蛋白质的副本组成，已由低分辨率电子显微镜结构的相扩展确定。衣壳蛋白具有一个突出的（P）结构域，该结构域通过柔性铰链连接到具有经典的八链p-sandwich基序的壳域。 P结构域的结构与任何其他病毒蛋白的结构不同，该病毒蛋白具有亚域的折叠，类似于真核翻译伸长因子TU中第二个域的折叠。该亚域位于衣壳的外部，在诺沃克状的人校 - 病毒中具有最大的序列变化，并且很可能包含应变特异性和细胞结合的决定因素。
Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure of a calicivirus capsid, which consists of 180 copies of a single protein, has been determined by phase extension from a Low-resolution electron microscopy structure. The capsid protein has a protruding (P) domain connected by a flexible hinge to a shell (S) domain that has a classical eight-stranded P-sandwich motif. The structure of the P domain is unlike that of any other viral protein with a subdomain exhibiting a fold similar to that of the second domain in the eukaryotic translation elongation factor-Tu. This subdomain, Located at the exterior of the capsid, has the Largest sequence variation among Norwalk-Like human calici-viruses and is Likely to contain the determinants of strain specificity and cell binding.