STRUCTURAL BASIS OF C TYPE LECTIN CARBOHYDRATE INTERACTION

C型动物凝集素是一个依赖于Ca 2+的大家族， 在细胞粘附中起作用的碳水化合物结合蛋白， 血清糖蛋白清除和宿主防御。 我们正在使用 高分辨率的X射线晶体学来了解 碳水化合物配体的弱但特异性识别的基础 通过这些蛋白质，以及它们的寡聚体组织， 将多价化合物的结合位点聚集在限定的几何形状中， 碳水化合物识别 我们也在研究pH依赖性 使C型凝集素不能结合的构象变化 钙和碳水化合物在温和的酸性pH值，一个属性， 这些C型凝集素的生物学中心， 受体。

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.