Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin).
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ABSTRACT:
SUBMITTER: Wiltzius JJ
PROVIDER: S-EPMC2525530 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
Publications
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin).
Wiltzius Jed J W JJ Sievers Stuart A SA Sawaya Michael R MR Cascio Duilio D Popov Dmitriy D Riekel Christian C Eisenberg David D
Protein science : a publication of the Protein Society 20080612 9
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 ...[more]
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