The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted β‐sheet flanked by α‐helices found in human ras‐p21

FEBS Letters

Perkins, Stephen J.¹  Edwards, Yvonne J.K.¹ 

[1] Department of Biochemistry and Molecular Biology, Royal Free Hospital School of Medicine, Rowland Hill Street, London NW3 2PF, UK

关键词: von Willebrand factor;    Doubly-wound α/β fold;    ras-p21;    Secondary structure prediction;    Protein fold recognition;    vWF domain;    von Willebrand factor type A domain;    EF-Tu;    elongation factor Tu;   

DOI  :  10.1016/0014-5793(94)01447-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 α-helices and six β-strands. A protein fold for this domain is proposed to correspond to a doubly-wound open twisted β-sheet structure flanked by α-helices. Close agreement was found with the GTP-binding domain of human ras-p21, provided that an extra α-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.

【 授权许可】

Unknown