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This Article ACCEPTED PREPRINT Full Text (PDF) Supplemental Research Data All Versions of this Article: ps.036509.108v1 17/9/1467    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Wiltzius, J. J.W. Articles by Eisenberg, D. PubMed PubMed Citation Articles by Wiltzius, J. J.W. Articles by Eisenberg, D. Social Bookmarking                   What's this?

Accelerated Communication

Atomic structure of the cross-β spine of Islet Amyloid Polypeptide (Amylin)

¹ UCLA;
² ESRF

(RECEIVED May 18, 2008; ACCEPTED June 10, 2008)

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: Crystallography; IAPP; aggregation; amyloid; type II diabetes

³ E-mail: jjww{at}ucla.edu

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