Atomic structure of the cross-[beta] spine of islet amyloid polypeptide (amylin)

Journal Article · Fri Mar 27 00:00:00 EDT 2009 · Protein Sci.

DOI:https://doi.org/10.1110/ps.036509.108· OSTI ID:1007073

Wiltzius, J J; Sievers, S A; Sawaya, M R; Cascio, D; Popov, D; Riekel, C; Eisenberg, D ^[1]

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1. UCLA

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.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: USDOE
• OSTI ID: 1007073
• Journal Information: Protein Sci., Vol. 17, Issue (9) ; 09, 2008
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
HUMAN POPULATIONS
HORMONES
POLYPEPTIDES
PANCREAS
DIABETES MELLITUS
MOLECULAR STRUCTURE