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Structural insight into nucleotide recognition by human death-associated protein kinase.

McNamara LK, Watterson DM, Brunzelle JS
Acta Crystallogr D Biol Crystallogr 65 241-8 (2009)
Related entries: 3eh9, 3f5g, 3f5u

Cited: 10 times
EuropePMC logo PMID: 19237746

Abstract

Death-associated protein kinase (DAPK) is a member of the Ca(2+)/calmodulin-regulated family of serine/threonine protein kinases. The role of the kinase activity of DAPK in eukaryotic cell apoptosis and the ability of bioavailable DAPK inhibitors to rescue neuronal death after brain injury have made it a drug-discovery target for neurodegenerative disorders. In order to understand the recognition of nucleotides by DAPK and to gain insight into DAPK catalysis, the crystal structure of human DAPK was solved in complex with ADP and Mg(2+) at 1.85 A resolution. ADP is a product of the kinase reaction and product release is considered to be the rate-limiting step of protein kinase catalytic cycles. The structure of DAPK-ADP-Mg(2+) was compared with a newly determined DAPK-AMP-PNP-Mg(2+) structure and the previously determined apo DAPK structure (PDB code 1jks). The comparison shows that nucleotide-induced changes are localized to the glycine-rich loop region of DAPK.

Articles - 3eha mentioned but not cited (2)

  1. Structural insight into nucleotide recognition by human death-associated protein kinase. McNamara LK, Watterson DM, Brunzelle JS. Acta Crystallogr D Biol Crystallogr 65 241-248 (2009)
  2. A Chemical Probe for Dark Kinase STK17B Derives Its Potency and High Selectivity through a Unique P-Loop Conformation. Picado A, Chaikuad A, Wells CI, Shrestha S, Zuercher WJ, Pickett JE, Kwarcinski FE, Sinha P, de Silva CS, Zutshi R, Liu S, Kannan N, Knapp S, Drewry DH, Willson TM. J Med Chem 63 14626-14646 (2020)


Reviews citing this publication (1)

  1. Death Associated Protein Kinase 1 (DAPK1): A Regulator of Apoptosis and Autophagy. Singh P, Ravanan P, Talwar P. Front Mol Neurosci 9 46 (2016)

Articles citing this publication (7)

  1. Chemical genetics of zipper-interacting protein kinase reveal myosin light chain as a bona fide substrate in permeabilized arterial smooth muscle. Moffat LD, Brown SB, Grassie ME, Ulke-Lemée A, Williamson LM, Walsh MP, MacDonald JA. J Biol Chem 286 36978-36991 (2011)
  2. Molecular features of product release for the PKA catalytic cycle. Bastidas AC, Wu J, Taylor SS. Biochemistry 54 2-10 (2015)
  3. Homodimerization of the death-associated protein kinase catalytic domain: development of a new small molecule fluorescent reporter. Zimmermann M, Atmanene C, Xu Q, Fouillen L, Van Dorsselaer A, Bonnet D, Marsol C, Hibert M, Sanglier-Cianferani S, Pigault C, McNamara LK, Watterson DM, Haiech J, Kilhoffer MC. PLoS One 5 e14120 (2010)
  4. Targeting Pim Kinases and DAPK3 to Control Hypertension. Carlson DA, Singer MR, Sutherland C, Redondo C, Alexander LT, Hughes PF, Knapp S, Gurley SB, Sparks MA, MacDonald JA, Haystead TAJ. Cell Chem Biol 25 1195-1207.e32 (2018)
  5. LASSBio-1829 Hydrochloride: Development of a New Orally Active N-Acylhydrazone IKK2 Inhibitor with Anti-inflammatory Properties. Guedes IA, Freitas RH, Cordeiro NM, do Nascimento TS, Valerio TS, Fernandes PD, Dardenne LE, Fraga CA. ChemMedChem 11 234-244 (2016)
  6. Triple resonance EPR spectroscopy determines the Mn2+ coordination to ATP. Litvinov A, Feintuch A, Un S, Goldfarb D. J Magn Reson 294 143-152 (2018)
  7. Site-directed mutagenesis of the glycine-rich loop of death associated protein kinase (DAPK) identifies it as a key structure for catalytic activity. McNamara LK, Brunzelle JS, Schavocky JP, Watterson DM, Grum-Tokars V. Biochim Biophys Acta 1813 1068-1073 (2011)


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