Three-dimensional structure of the tyrosine kinase c-Src View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-02

AUTHORS

Wenqing Xu, Stephen C. Harrison, Michael J. Eck

ABSTRACT

The structure of a large fragment of the c-Src tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tail, has been determined at 1.7 Å resolution in a closed, inactive state. Interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. More... »

PAGES

595-602

Journal

TITLE

Nature

ISSUE

6617

VOLUME

385

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/385595a0

    DOI

    http://dx.doi.org/10.1038/385595a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1032796118

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9024657


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