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Human Protein Tyrosine Kinase 2 Beta

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PDB Code 3CC6 Target Class Protein Kinase Target PTK2B Alias CADTK, CAKB, FADK2, FAK2, FRNK, PKB, PTK, PTK2B, PYK2, RAFTK Disease Area/Function metabolism Date Deposited Feb 25 2008 Authors R.D.BUSAM, L.LEHTIO, T.KARLBERG, C.H.ARROWSMITH, C.BOUNTRA, R.COLLINS, L.G.DAHLGREN, A.M.EDWARDS, S.FLODIN, A.FLORES, S.GRASLUND, M.HAMMARSTROM, T.HELLEDAY, M.D.HERMAN, A.JOHANSSON, I.JOHANSSON, A.KALLAS, T.KOTENYOVA, M.MOCHE, M.E.NILSSON, P.NORDLUND, T.NYMAN, C.PERSSON, J.SAGEMARK, L.SVENSSON, A.G.THORSELL, L.TRESAUGUES, S.VAN DEN BERG, J.WEIGELT, M.WELIN, H.BERGLUND

About this structure

Kinases are enzymes critical in signaling pathways. Protein tyrosine kinase 2 beta is a cytoplasmic kinase which catalyzes the reaction of ATP + [protein]-L-tyrosine -> ADP + [protein]-L-tyrosine phosphate. It is a member of the focal adhesion kinase (FAK) subfamily. FAK proteins are involved in processes of motility and cell adhesion and are often associated with a variety of cancers. The protein is involved in the activation of the mitogen-activated kinase (MAP) signaling pathway as well as calcium-induced regulation of ion channels. This protein has been shown to bind CRK-associated substrate, nephrocystin, Rap GTPase, and the SH2 domain of GRB2. PTK2B consists of 3 distinct domains: A N-terminal Protein 4.1, Ezrin, Radixin, Moesin (FERM) domain, a central FAK domain, and a Focal Adhesion Targeting (FAT) domain. The crystal structure of the PTK2B FAK domain is presented here at 1.6 Å resolution.

References

  1. Lev, S., et al. (1995) Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature 376, 737-45.
  2. Dikic, I., et al. (1996) A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383, 547-50.
  3. Benzing, T., et al. (2001) Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers phosphorylation of Pyk2. PNAS 98, 9784-9.
  4. McLeod, S.J., et al. (2004) The Rap GTPases Regulate Integrin-mediated Adhesion, Cell Spreading, Actin Polymerization, and Pyk2 Tyrosine Phosphorylation in B Lymphocytes. J. Biol. Chem. 279, 12009-12019.