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Article

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils.

Nature structural & molecular biology - 1 Jul 2020

Cao Qin, Boyer David R, Sawaya Michael R, Ge Peng, Eisenberg David S

Abstract excerpt

Human islet amyloid polypeptide (hIAPP) functions as a glucose-regulating hormone but deposits as amyloid fibrils in more than 90% of patients with type II diabetes (T2D). Here we report the cryo-EM structure of recombinant full-length hIAPP fibrils. The fibril is composed of two symmetrically related protofilaments with ordered residues 14-37. Our hIAPP fibril structure (i) supports the previous hypothesis that...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 32541896
DOI: 10.1038/s41594-020-0435-3
PMCID: PMC8579859

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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