Crystal structure of the tyrosine kinase domain of the human insulin receptor
- PMID: 7997262
- DOI: 10.1038/372746a0
Crystal structure of the tyrosine kinase domain of the human insulin receptor
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.
Comment in
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Signal transduction. Look at a tyrosine kinase.Nature. 1994 Dec 22-29;372(6508):726-7. doi: 10.1038/372726a0. Nature. 1994. PMID: 7997256 No abstract available.
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