Reference: Xu W, et al. (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature 385(6617):595-602

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Abstract


The structure of a large fragment of the c-Src tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tall, has been determined at 1.7 A 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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Xu W, Harrison SC, Eck MJ
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