Three-dimensional structure of the tyrosine kinase c-Src

Wenqing Xu, Stephen C. Harrison and Michael J. Eck
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Wenqing Xu: Children's Hospital
Stephen C. Harrison: Children's Hospital
Michael J. Eck: Children's Hospital

Nature, 1997, vol. 385, issue 6617, 595-602

Abstract: 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.

Date: 1997
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DOI: 10.1038/385595a0

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