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Nature. 1997 Feb 13;385(6617):595-602.

Three-dimensional structure of the tyrosine kinase c-Src.

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1
Laboratory of Molecular Medicine, Children's Hospital, Boston, Massachusetts 02115, USA.

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.

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PMID:
9024657
DOI:
10.1038/385595a0
[Indexed for MEDLINE]
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