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Article
Nature 372, 746-754 (29 December 1994) | doi:10.1038/372746a0; Accepted 17 November 1994
Crystal structure of the tyrosine kinase domain of the human insulin receptor
Stevan R. Hubbard*, Lei Wei† & Wayne A. Hendrickson*‡
- *, Department of Biochemistry and Molecular Biophysics, and ‡Howard Hughes Medical Institute, Columbia University, New York, New York 10032, USA
- †W. M. Keck Center for Genome Informatics, Institute of Biosciences and Technology, Texas A & M University, Houston, Texas 77030, USA
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 Å 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.
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