STRUCTURAL STUDIES OF LUNG SURFACTANT PROTEIN

肺表面活性蛋白A是肺表面活性物质的重要结构成分， 哺乳动物的肺 这种蛋白质的羧基末端结构域 在中性pH和存在下识别并结合碳水化合物 Ca2+。 该结构域还显示出与所述结构域的显著序列相似性。 其他动物凝集素的碳水化合物识别结构域， 中性pH和Ca2+结合碳水化合物。 精确的函数和 肺组织碳水化合物识别结构域（CRD）的作用机制 表面活性蛋白A是未知，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着重要作用， 肺的完整性以及在清除肺的入侵 病原体是存在的。 这个项目的目标是定义一个 分子水平的结构基础，这些观察到的功能，通过 人CRD的X射线晶体结构测定， 大鼠和小鼠肺表面活性蛋白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 the lung of invading 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.