HUMAN PLASMA PLATELET ACTIVATING FACTOR ACETYLHYDROLASE

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 血浆形式的人血小板活化因子乙酰水解酶(PPAFAH)通过降低PAF水平起到一般抗炎清除剂的作用，并与过敏性休克、哮喘和过敏反应有关。作为一种膜相关蛋白，pPAFAH没有已知的同源物，是一个有价值的结构靶点。最近，我们已经发表了这种重要酶的晶体结构，并展示了酶如何在催化过程中与低密度脂蛋白界面结合。从24ID获得的数据将被用来解析pPAFAH与沙林和梭曼的络合物的晶体结构，并有助于预测底物与酶的结合方式和有毒有机磷的水解。 以24ID采集数据的复杂结构的PDB代码为3F96和 沙林和梭曼分别为3F97。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The plasma form of human platelet activating factor acetylhydrolase (pPAFAH) functions by reducing PAF levels as a general anti-inflammatory scavenger and is linked to anaphylactic shock, asthma and allergic reactions. As a membrane associated protein with no known homologues, pPAFAH is a worthy structural target. Recently we have published the crystal structure of this important enzyme and shown how enzyme binds to LDL interface during catalysis. Data collected from 24ID would be used to solve the crystal structures of pPAFAH complex with sarin and soman and useful to predict the mode of substrate binding to the enzyme and hydrolysis of toxic organophosphates. PDB codes for the complex structures for which data collected at 24ID are 3F96 and 3F97 for sarin and soman, respectively.