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2W4K

X-ray structure of a DAP-Kinase 2-302

Summary for 2W4K
Entry DOI10.2210/pdb2w4k/pdb
Related1IG1 1JKK 1JKL 1JKS 1JKT 1P4F 2JL2 2W4J 2XUU 4B4L
DescriptorDEATH-ASSOCIATED PROTEIN KINASE 1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordspolymorphism, phosphoprotein, calmodulin-binding, serine/threonine-protein kinase, nucleotide-binding, alternative splicing, dapk, kinase, complex, apoptosis, cytoplasm, ank repeat, calmodulin, transferase, atp-binding
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationIsoform 1: Cytoplasm. Isoform 2: Cytoplasm: P53355
Total number of polymer chains1
Total formula weight35147.16
Authors
De Diego, I.,Kuper, J.,Lehmann, F.,Wilmanns, M. (deposition date: 2008-11-27, release date: 2009-12-22, Last modification date: 2023-12-13)
Primary citationTemmerman, K.,De Diego, I.,Pogenberg, V.,Simon, B.,Jonko, W.,Li, X.,Wilmanns, M.
A Pef/Y Substrate Recognition and Signature Motif Plays a Critical Role in Dapk-Related Kinase Activity.
Chem.Biol., 21:264-, 2014
Cited by
PubMed Abstract: Knowledge about protein kinase substrate preferences is biased toward residues immediately adjacent to the site of phosphorylation. By a combined structural, biochemical, and cellular approach, we have discovered an unexpected substrate recognition element with the consensus sequence PEF/Y in the tumor suppressor death-associated protein kinase 1. This motif can be effectively blocked by a specific pseudosubstrate-type interaction with an autoregulatory domain of this kinase. In this arrangement, the central PEF/Y glutamate interacts with a conserved arginine distant to the phosphorylation site in sequence and structure. We also demonstrate that the element is crucial for kinase activity regulation and substrate recognition. The PEF/Y motif distinguishes close death-associated protein kinase relatives from canonical calcium/calmodulin-dependent protein kinases. Insight into this signature and mode of action offers new opportunities to identify specific small molecule inhibitors in PEF/Y-containing protein kinases.
PubMed: 24440081
DOI: 10.1016/J.CHEMBIOL.2013.12.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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