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3EHA

Crystal structure of death associated protein kinase complexed with AMPPNP

Summary for 3EHA
Entry DOI10.2210/pdb3eha/pdb
Related1EH9 1JKK 1JKL 1JKS 1ig1
DescriptorDeath-associated protein kinase 1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
Functional Keywordskinase domain s/t kinase, ank repeat, apoptosis, atp-binding, calmodulin-binding, cytoplasm, kinase, nucleotide-binding, phosphoprotein, polymorphism, serine/threonine-protein kinase, transferase
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm: P53355
Total number of polymer chains1
Total formula weight34300.56
Authors
McNamara, L.K.,Watterson, D.M.,Brunzelle, J.S. (deposition date: 2008-09-11, release date: 2009-04-28, Last modification date: 2023-08-30)
Primary citationMcNamara, L.K.,Watterson, D.M.,Brunzelle, J.S.
Structural insight into nucleotide recognition by human death-associated protein kinase.
Acta Crystallogr.,Sect.D, 65:241-248, 2009
Cited by
PubMed 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.
PubMed: 19237746
DOI: 10.1107/S0907444908043679
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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