首页 | 本学科首页   官方微博 | 高级检索  
     


Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)
Authors:Wiltzius Jed J W  Sievers Stuart A  Sawaya Michael R  Cascio Duilio  Popov Dmitriy  Riekel Christian  Eisenberg David
Affiliation:Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, California 90095-1570, USA.
Abstract:Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid-like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full-length IAPP polymorph.
Keywords:IAPP   amylin   amyloid   aggregation   type 2 diabetes   protein crystallization
本文献已被 PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号