| Literature DB >> 7997262 |
S R Hubbard1, L Wei, L Ellis, W A Hendrickson.
Abstract
The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 A resolution. The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.Entities:
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Year: 1994 PMID: 7997262 DOI: 10.1038/372746a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962