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Cryo electron microscopy of recombinant, un-seeded hIAPP fibrils

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SUBMITTER: Qin Cao 

PROVIDER: EMPIAR-10871 | biostudies-other |

REPOSITORIES: biostudies-other

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

Cao Qin Q   Boyer David R DR   Sawaya Michael R MR   Ge Peng P   Eisenberg David S DS  

Nature structural & molecular biology 20200615 7

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 residues 20-29 constitute the core of the hIAPP amyloid; (ii) suggests a molecular m  ...[more]

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