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西尼罗河病毒核心蛋白;四聚体结构与带状物形成。

West Nile virus core protein; tetramer structure and ribbon formation.

作者信息

Dokland Terje, Walsh Martin, Mackenzie Jason M, Khromykh Alexander A, Ee Kim-Huey, Wang Sifang

机构信息

Institute of Molecular and Cell Biology, Singapore, Republic of Singapore.

出版信息

Structure. 2004 Jul;12(7):1157-63. doi: 10.1016/j.str.2004.04.024.

Abstract

We have determined the crystal structure of the core (C) protein from the Kunjin subtype of West Nile virus (WNV), closely related to the NY99 strain of WNV, currently a major health threat in the U.S. WNV is a member of the Flaviviridae family of enveloped RNA viruses that contains many important human pathogens. The C protein is associated with the RNA genome and forms the internal core which is surrounded by the envelope in the virion. The C protein structure contains four alpha helices and forms dimers that are organized into tetramers. The tetramers form extended filamentous ribbons resembling the stacked alpha helices seen in HEAT protein structures.

摘要

我们已经确定了西尼罗河病毒(WNV)昆金亚型核心(C)蛋白的晶体结构,该亚型与WNV的NY99毒株密切相关,目前是美国的主要健康威胁。WNV是黄病毒科包膜RNA病毒家族的成员,该家族包含许多重要的人类病原体。C蛋白与RNA基因组相关联,并形成内部核心,该核心在病毒粒子中被包膜包围。C蛋白结构包含四个α螺旋,并形成二聚体,这些二聚体又组成四聚体。这些四聚体形成延伸的丝状带,类似于在HEAT蛋白结构中看到的堆叠α螺旋。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5ea/7173237/7157bf5b15b5/gr1_lrg.jpg

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