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A Membrane‐Bound Antiparallel Dimer of Rat Islet Amyloid Polypeptide
Author(s) -
Nath Abhinav,
Miranker Andrew D.,
Rhoades Elizabeth
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201102887
Subject(s) - antiparallel (mathematics) , dimer , islet , amyloid (mycology) , chemistry , gene isoform , crystallography , biophysics , computational biology , computer science , biochemistry , biology , physics , gene , endocrinology , diabetes mellitus , organic chemistry , quantum mechanics , inorganic chemistry , magnetic field
Gaining recognition : The structure of a previously unrecognized antiparallel dimer of rat islet amyloid polypeptide bound to anionic membrane nanodiscs was examined by using a combination of single‐pair FRET and Rosetta model refinement. Models of the dimer showed a likely interface for lipid binding and suggest key interactions may also occur in the human isoform, thereby providing possible insights into fibril formation in type II diabetes.
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