CRYSTAL STRUCTURE OF VON WILLEBRAND FACTOR A1 DOMAIN

说明：这是一个建议，以确定和研究这三个- 人血管性血友病因子（vWF）A1结构域的三维结构 因子 A1结构域负责结合血小板 糖蛋白GP 1b受体复合物，从而激活血小板 聚合来 与天然vWF的结合仅在高剪切下发生 条件下或当因素被吸收到表面，但孤立的 At结构域在溶液相中结合GP 1b。 某些遗传形式的 血管性血友病图作为单一置换突变内 A1结构域。 因此，这个域的结构将揭示一个 它的许多重要的生物学和病理学功能 分子。

DESCRIPTION: This is a proposal to determine and study the three- dimensional structure of the A1 domain of human von Willebrand (vWF) factor. The A1 domain is responsible for binding the platelet glycoprotein GPlb receptor complex and thereby activating platelet aggregation. Binding to native vWF only occurs under high shear conditions or when the factor is absorbed to surfaces, but the isolated At domain binds GPlb in the solution phase. Certain heritable forms of von Willebrand's disease map as single substitution mutations within the A1 domain. Thus, the structure of this domain will shed light on a number of important biological and pathological functions of this molecule.