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Crystal structure of the Src family tyrosine kinase Hck

Author

Listed:
  • Frank Sicheri
  • Ismail Moarefi

    (The Rockefeller University
    The Rockefeller University)

  • John Kuriyan

    (The Rockefeller University
    The Rockefeller University)

Abstract

The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 Å resolution. Inhibition of enzymatic activity is a consequence of intramolecular interactions of the enzyme's Src-homology domains SH2 and SH3, with concomitant displacement of elements of the catalytic domain. The conformation of the active site has similarities with that of inactive cyclin-dependent protein kinases.

Suggested Citation

  • Frank Sicheri & Ismail Moarefi & John Kuriyan, 1997. "Crystal structure of the Src family tyrosine kinase Hck," Nature, Nature, vol. 385(6617), pages 602-609, February.
    • Handle: RePEc:nat:nature:v:385:y:1997:i:6617:d:10.1038_385602a0
    DOI: 10.1038/385602a0
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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. 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.
    3. Trayder Thomas & Benoît Roux, 2021. "Tyrosine kinases: complex molecular systems challenging computational methodologies," The European Physical Journal B: Condensed Matter and Complex Systems, Springer;EDP Sciences, vol. 94(10), pages 1-13, October.

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