STRUCTURAL BASIS OF C TYPE LECTIN CARBOHYDRATE INTERACTION

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。

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.