THE PROTEIN FOLD OF THE VON-WILLEBRAND-FACTOR TYPE-A DOMAIN IS PREDICTED TO BE SIMILAR TO THE OPEN TWISTED BETA-SHEET FLANKED BY ALPHA-HELICES FOUND IN HUMAN RAS-P21

被引：34

作者：

EDWARDS, YJK ^{[1
]}

PERKINS, SJ ^{[1
]}

机构：

[1] ROYAL FREE HOSP,SCH MED,DEPT BIOCHEM & MOLEC BIOL,LONDON NW3 2PF,ENGLAND

来源：

FEBS LETTERS | 1995年 / 358卷 / 03期

基金：

英国惠康基金;

关键词：

VON WILLEBRAND FACTOR; DOUBLY-WOUND ALPHA/BETA FOLD; RAS-P21; SECONDARY STRUCTURE PREDICTION; PROTEIN FOLD RECOGNITION;

D O I：

10.1016/0014-5793(94)01447-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The von Willebrand Factor type A domain is the prototype for a protein superfamily. It possesses no significant sequence similarity to any known protein structure. Secondary structure predictions indicate a largely alternating pattern of six alpha-helices and six beta-strands. A protein fold for this domain is proposed to correspond to a doubly-wound open twisted beta-sheet structure flanked by alpha-helices. Close agreement was found with the GTP-binding domain of human ras-p21, provided that an extra alpha-helix was inserted. The structure of the predicted fold showed high compatibility with the proximate location of two Mg2+-binding Asp residues, two disulphide-bridged Cys residues, and other known functional attributes of this domain.

引用

页码：283 / 286

页数：4

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