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Three-dimensional structure of the tyrosine kinase c-Src

Author

Listed:
  • Wenqing Xu

    (Children's Hospital
    Departments of Microbiology and Molecular Genetics)

  • Stephen C. Harrison

    (Children's Hospital
    Departments of Biological Chemistry and Molecular Pharmacology
    Departments of Pediatrics
    The Howard Hughes Medical Institute)

  • Michael J. Eck

    (Children's Hospital
    Departments of Biological Chemistry and Molecular Pharmacology)

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.

Suggested Citation

  • Wenqing Xu & Stephen C. Harrison & Michael J. Eck, 1997. "Three-dimensional structure of the tyrosine kinase c-Src," Nature, Nature, vol. 385(6617), pages 595-602, February.
    • Handle: RePEc:nat:nature:v:385:y:1997:i:6617:d:10.1038_385595a0
    DOI: 10.1038/385595a0
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    Cited by:

    1. Sichun Yang & Benoît Roux, 2008. "Src Kinase Conformational Activation: Thermodynamics, Pathways, and Mechanisms," PLOS Computational Biology, Public Library of Science, vol. 4(3), pages 1-14, March.
    2. Hipólito Nicolás Cuesta-Hernández & Julia Contreras & Pablo Soriano-Maldonado & Jana Sánchez-Wandelmer & Wayland Yeung & Ana Martín-Hurtado & Inés G. Muñoz & Natarajan Kannan & Marta Llimargas & Javie, 2023. "An allosteric switch between the activation loop and a c-terminal palindromic phospho-motif controls c-Src function," Nature Communications, Nature, vol. 14(1), pages 1-21, December.
    3. Zhenxi Li & Xinghai Yang & Ruifeng Fu & Zhipeng Wu & Shengzhao Xu & Jian Jiao & Ming Qian & Long Zhang & Chunbiao Wu & Tianying Xie & Jiqiang Yao & Zhixiang Wu & Wenjun Li & Guoli Ma & Yu You & Yihua , 2024. "Kisspeptin-10 binding to Gpr54 in osteoclasts prevents bone loss by activating Dusp18-mediated dephosphorylation of Src," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    4. Nicole Dölker & Maria W Górna & Ludovico Sutto & Antonio S Torralba & Giulio Superti-Furga & Francesco L Gervasio, 2014. "The SH2 Domain Regulates c-Abl Kinase Activation by a Cyclin-Like Mechanism and Remodulation of the Hinge Motion," PLOS Computational Biology, Public Library of Science, vol. 10(10), pages 1-12, October.

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