24小时热门版块排行榜

返回列表

【奖励】本帖被评价14次，作者myprayer增加金币 11 个

myprayer

专家顾问 (著名写手)

[资源] 《自然》【nature】2013年1月3日全文PDF版本

清华大学施一公教授的文章
Structure of a presenilin family intramembrane aspartate protease
Xiaochun Li1,2*, Shangyu Dang1,2*, Chuangye Yan1,2, Xinqi Gong1,2, JiaweiWang2,3 & Yigong Shi1,2
Presenilin and signal peptide peptidase (SPP) are intramembrane aspartyl proteases that regulate important biologicalfunctions in eukaryotes.Mechanisticunderstandingof presenilin and SPPhas been hamperedby relevantstructuralinformation.Herewereport the crystal structure of a presenilin/SPPhomologue (PSH) fromthearchaeonMethanoculleusmarisnigri JR1. The protease, comprising nine transmembrane segments (TMs), adopts a previously unreported protein. The amino-terminal domain, consisting of TM1–6, forms a horseshoe-shaped structure, surrounding TM7–9 of thecarboxy-terminal domain. The two catalytic aspartate residues are located on the cytoplasmic side of TM6 and TM7,spatially close to each other and approximately 8A˚ into the lipid membrane surface. Water molecules gain constantaccess to the catalytic aspartates through a large cavity between the amino- and carboxy-terminal domains. Structuralanalysis reveals insights into the presenilin/SPP family of intramembrane proteases.
文章摘要

回复此楼

» 本帖附件资源列表

欢迎监督和反馈：小木虫仅提供交流平台，不对该内容负责。
本内容由用户自主发布，如果其内容涉及到知识产权问题，其责任在于用户本人，如对版权有异议，请联系邮箱：xiaomuchong@tal.com
附件 1 : Nature2013-1-3.pdf

2013-01-04 19:34:43, 32.71 M

» 收录本帖的淘帖专辑推荐

科研资料	文献推荐	生物类电子书	科技
都是好东西	项目、论文发表与收录	学术资源-Biology	Top Journals-BioMed
CNS杂志	我的淘贴	资源收藏	我喜欢
梦想路上	有用的东东