STRUCTURAL BASIS OF C TYPE LECTIN CARBOHYDRATE INTERACTION

C 型凝集素碳水化合物相互作用的结构基础

• 批准号: 6586555
• 负责人: William I Weis
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586555
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; proteins; radiography; structural biology

C-type animal lectins are a large family of Ca2+ -dependent carbohydrate-binding proteins that function in cellular adhesion, serum glycoprotein clearance and host defense. We are using high-resolution x-ray crystallography to understand the structural basis of the weak, but specific, recognition of carbohydrate ligands by these proteins, as well as their oligomeric organization that clusters binding sites in a defined geometry for multivalent carbohydrate recognition. We are also studying the pH-dependent conformational change that renders C-type lectins unable to bind calcium and hence carbohydrates at mildly acid pH, a property which is central to the biology of those C-type lectins that serve as endocytic receptors.

C型动物凝集素是一个依赖钙离子的大家族 在细胞黏附中起作用的碳水化合物结合蛋白， 血清糖蛋白清除与宿主防御。我们正在使用 用高分辨率X射线结晶学来了解晶体结构 对碳水化合物配体的微弱但特异的识别基础 通过这些蛋白质以及它们的寡聚体组织 在定义的几何构型中聚集多价结合位点 碳水化合物识别。我们还在研究依赖于pH的 使C型凝集素无法结合的构象变化 钙，因此碳水化合物在中等酸性的pH下，这一性质是 作为内吞的C型凝集素的生物学中心 感受器。