Edwards Y J, Perkins S J
Department of Biochemistry and Molecular Biology, Royal Free Hospital School of Medicine, London, UK.
FEBS Lett. 1995 Jan 30;358(3):283-6. doi: 10.1016/0014-5793(94)01447-9.
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 Mg(2+)-binding Asp residues, two disulphide-bridged Cys residues, and other known functional attributes of this domain.
血管性血友病因子 A 结构域是一个蛋白质超家族的原型。它与任何已知的蛋白质结构都没有显著的序列相似性。二级结构预测表明，它主要是由六个α螺旋和六个β链交替排列组成。该结构域的蛋白质折叠被认为对应于一种两侧有α螺旋的双缠绕开放扭曲β折叠结构。如果插入一个额外的α螺旋，则发现它与人类ras-p21的GTP结合结构域高度一致。预测折叠结构与该结构域两个结合Mg(2+)的天冬氨酸残基、两个二硫键连接的半胱氨酸残基的临近位置以及其他已知功能属性具有高度兼容性。
