CRYSTAL STRUCTURE OF VON WILLEBRAND FACTOR A1 DOMAIN

血管性血友病因子 A1 结构域的晶体结构

• 批准号: 2638056
• 负责人: KOTTAYIL I VARUGHESE
• 金额: $ 22.81万
• 依托单位: SCRIPPS RESEARCH INSTITUTE, THE
• 依托单位国家: 美国
• 财政年份: 1996
• 资助国家: 美国
• 起止时间: 1996-01-01 至 1998-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2638056
• 关键词: X ray crystallography; crystallization; glycoproteins; molecular site; monoclonal antibody; mutant; platelet aggregation; protein structure function; recombinant proteins; structural biology; von Willebrand factor

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.

描述：这是一项确定和研究三个方面的建议- 人von Willebrand(VWF)A1结构域的空间结构 因素。A1结构域负责与血小板结合 糖蛋白GPlb受体复合体从而激活血小板 聚合。仅在高剪切力下才会绑定到本地vWF 条件或当因子被吸收到表面时，但孤立的 AT结构域在解决阶段与GPlb结合。某些可遗传的形式 Von Willebrand疾病图谱中的单替换突变 A1域。因此，这个领域的结构将揭示一个 其重要的生物学和病理功能 分子。