2W4K
X-ray structure of a DAP-Kinase 2-302
Summary for 2W4K
Entry DOI | 10.2210/pdb2w4k/pdb |
Related | 1IG1 1JKK 1JKL 1JKS 1JKT 1P4F 2JL2 2W4J 2XUU 4B4L |
Descriptor | DEATH-ASSOCIATED PROTEIN KINASE 1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | polymorphism, phosphoprotein, calmodulin-binding, serine/threonine-protein kinase, nucleotide-binding, alternative splicing, dapk, kinase, complex, apoptosis, cytoplasm, ank repeat, calmodulin, transferase, atp-binding |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Isoform 1: Cytoplasm. Isoform 2: Cytoplasm: P53355 |
Total number of polymer chains | 1 |
Total formula weight | 35147.16 |
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 citation | Temmerman, 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: 24440081DOI: 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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