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.
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Xu, W., Harrison, S. & Eck, M. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595–602 (1997). https://doi.org/10.1038/385595a0
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DOI: https://doi.org/10.1038/385595a0
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