Download MendeleyThree-dimensional structure of the tyrosine kinase c-Src.
Xu, W., Harrison, S.C., Eck, M.J.(1997) Nature 385: 595-602
- PubMed: 9024657
- DOI: https://doi.org/10.1038/385595a0
- Primary Citation of Related Structures:
1FMK - PubMed 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.
Organizational Affiliation:
Laboratory of Molecular Medicine, Children's Hospital, Boston, Massachusetts 02115, USA.
