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Structure of the insulin receptor ectodomain reveals a folded-over conformation

Structure of the insulin receptor ectodomain reveals a folded-over conformation The first report of the crystal structure of the whole insulin receptor ectodomain dimer reveals how its multiple domains are organized. The structure also identifies the elusive second binding site on the receptor, and suggests how the high-affinity insulin–receptor complex, which leads to signal induction, is generated. The structure as now published differs dramatically from previous versions based on reconstructions from cryoelectron microscopy data. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

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References (35)

Publisher
Springer Journals
Copyright
Copyright © 2006 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/nature05106
Publisher site
See Article on Publisher Site

Abstract

The first report of the crystal structure of the whole insulin receptor ectodomain dimer reveals how its multiple domains are organized. The structure also identifies the elusive second binding site on the receptor, and suggests how the high-affinity insulin–receptor complex, which leads to signal induction, is generated. The structure as now published differs dramatically from previous versions based on reconstructions from cryoelectron microscopy data.

Journal

NatureSpringer Journals

Published: Sep 6, 2006

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