STRUCTURAL STUDIES OF LUNG SURFACTANT PROTEIN

肺表面活性物质蛋白A是肺表面活性物质的重要结构成分 哺乳动物的肺。该蛋白质的羧基末端结构域 在中性pH和存在的情况下识别和结合碳水化合物 Ca2+。该结构域还显示出与 其他动物凝集素的碳水化合物识别结构域 中性pH和钙离子与碳水化合物结合。精确的函数和 肺糖识别结构域(CRD)的作用机制 表面活性蛋白A是未知的，然而有证据表明这种蛋白 在建立和维护体系结构方面发挥作用 肺的完整性以及清除病原体的完整性确实存在。 这个项目的目标是定义一种分子级的结构 通过X射线结晶学观察到的这些功能的基础 人、大鼠和小鼠肺CRD的结构测定 表面活性蛋白A。

Lung surfactant protein A is an important structural component of mammalian lungs. The carboxy terminal domain of this protein recognizes and binds carbohydrate at neutral pH and in the presence of Ca2+. This domain also shows significant sequence similarity to the carbohydrate recognition domains of other animal lectins which require neutral pH and Ca2+ to bind carbohydrate. The precise function and mechanisms of the carbohydrate recognition domain (CRD) of lung surfactant protein A are unknown, however evidence that this protein plays a role in establishing and maintaining the architectural integrity of the lung as well as in clearing pathogens does exist. The goal of this project is to define a molecular-level structural basis for these observed functions via the X-ray crystallographic structure determination of the CRD of human, rat, and mouse lung surfactant protein A.