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番茄丛矮病毒外壳蛋白的突出结构域是一类迄今未被识别的果冻卷构象。

Protruding domain of tomato bushy stunt virus coat protein is a hitherto unrecognized class of jellyroll conformation.

作者信息

Gibson T J, Argos P

机构信息

European Molecular Biology Laboratory, Heidelberg, F.R.G.

出版信息

J Mol Biol. 1990 Mar 5;212(1):7-9. doi: 10.1016/0022-2836(90)90298-Z.

Abstract

The capsid protein of tomato bushy stunt virus (TBSV) has two antiparallel beta-sheet domains with the so-called jellyroll conformation. Contrary to previous analyses, we note that these domains are non-superimposable topologies. The TBSV shell (S) domain topology is common to many other proteins but the protruding (P) domain is a unique conformation so far found in no other protein. The TBSV capsid P domain did not arise from the S domain by a gene duplication event as previously assumed. It is proposed instead that the P domain was acquired from an as yet unidentified cellular protein. The four possible unique jellyroll topologies that might occur in proteins are discussed and illustrated.

摘要

番茄丛矮病毒(TBSV)的衣壳蛋白有两个具有所谓“果冻卷”构象的反平行β-折叠结构域。与之前的分析不同,我们注意到这些结构域具有不可重叠的拓扑结构。TBSV的外壳(S)结构域拓扑结构在许多其他蛋白质中很常见,但突出(P)结构域是迄今为止在其他蛋白质中未发现的独特构象。TBSV衣壳P结构域并非如之前所认为的那样通过基因复制事件从S结构域产生。相反,有人提出P结构域是从一种尚未鉴定的细胞蛋白中获得的。文中讨论并说明了蛋白质中可能出现的四种独特的果冻卷拓扑结构。

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