STRUCTURAL STUDY OF INTRAMEMBRANE PROTEASES

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 早老素是γ-分泌酶的催化亚基，参与淀粉样前体蛋白的膜内加工，产生阿尔茨海默病的β-淀粉样蛋白。的疾病。为了了解早老素的催化机制，我们选择了一组活性位点序列基序高度相似的原核蛋白进行结构研究。这些蛋白负责去除N端信号肽，然后促进对靶蛋白的进一步加工。这组膜内蛋白酶的高分辨率结构将有助于更好地了解早老素的机制，早老素是阿尔茨海默病的关键参与者。的疾病。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Presenilin is the catalytic subunit of gamma-secretase involved in the intramemebranous processing of amyloid precursor protein, producing beta-amyloid protein of Alzheimer?s disease. In order to understand the catalytic mechanism of presenilin, a group of prokaryotic proteins containing highly similar active site sequence motif, was selected for structural studies. These proteins are responsible for removing the N terminal signal peptide and then facilitating the further processing for target proteins. The high-resolution structure of this group of intramembrane proteases will aid a better understanding of the mechanism of presenilin, a key player in Alzheimer?s disease.