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Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)
Author(s) -
Wiltzius Jed J.W.,
Sievers Stuart A.,
Sawaya Michael R.,
Cascio Duilio,
Popov Dmitriy,
Riekel Christian,
Eisenberg David
Publication year - 2008
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.036509.108
Subject(s) - amylin , islet , amyloid fibril , amyloid (mycology) , chemistry , fibril , residue (chemistry) , biophysics , biochemistry , crystallography , endocrinology , amyloid β , biology , medicine , insulin , inorganic chemistry , disease
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.