PRESEQUENCE PEPTIDASE IN NATIVE OR COMPLEXED WITH SUBSTRATES

天然或与底物复合的前序列肽酶

• 批准号: 7956813
• 负责人: WEI-JEN TANG
• 金额: $ 0.47万
• 依托单位: UNIVERSITY OF CHICAGO
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-08-01 至 2010-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7956813
• 关键词: Alzheimer' s Disease; Amyloid beta-Protein; Biochemical; Complex; Computer Retrieval of Information on Scientific Projects Database; Coupled; Funding; Grant; Homologous Gene; Homology Modeling; Human; Institution; Metalloproteases; Mitochondria; Peptide Hydrolases; Peptides; Plants; Play; Research; Research Personnel; Resources; Role; Source; United States National Institutes of Health; Zinc; structural biology; therapeutic development

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. Presequence peptidase (PreP) is a 117-kDa zinc metalloprotease that degrades amyloid-beta (Aβ), a peptide implicated in Alzheimer?s disease. Additionally, PreP has been postulated to regulate mitochondrial targeting sequences after import into the matrix. Structural studies from the plant homolog, AtPreP, and homology modeling suggest that human PreP possesses an inner chamber (crypt) that may play a role in substrate selectivity. Coupled with biochemical studies, the suitability of this protease for therapeutic development towards Alzheimer?s disease will be greatly enhanced by structural studies that give an enhanced understanding of the mechanisms of how PreP selects and degrades its substrates.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 前序列肽酶（PreP）是一种117 kDa的锌金属蛋白酶，可降解淀粉样蛋白β（A），一种与阿尔茨海默病有关的肽。的疾病。 此外，PreP已被假定为在导入基质后调节线粒体靶向序列。 植物同源物AtPreP的结构研究和同源性建模表明，人PreP具有内室（隐窝），可能在底物选择性中发挥作用。 再加上生化研究，这种蛋白酶对阿尔茨海默病治疗发展的适用性？的疾病将大大加强结构研究，使一个增强的了解机制，如何PreP选择和降解其基板。