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Published online before print June 12, 2008, 10.1110/ps.036509.108
Protein Science (2008), 17:1467-1474. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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ACCELERATED COMMUNICATION

Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)

Jed J.W. Wiltzius1, Stuart A. Sievers1, Michael R. Sawaya1, Duilio Cascio1, Dmitriy Popov2, Christian Riekel2, and David Eisenberg1

1 Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, California 90095-1570, USA
2 European Synchrotron Radiation Facility, BP 220, F-38043 Grenoble Cedex, France

(RECEIVED May 18, 2008; FINAL REVISION June 9, 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: IAPP; amylin; amyloid; aggregation; type 2 diabetes; protein crystallization


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