Crystal structure of the tyrosine kinase domain of the human insulin receptor View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-12

AUTHORS

S R Hubbard, 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. More... »

PAGES

746-754

Journal

TITLE

Nature

ISSUE

6508

VOLUME

372

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/372746a0

    DOI

    http://dx.doi.org/10.1038/372746a0

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/7997262


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