PDBsum entry 2x0g

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protein ligands metals Protein-protein interface(s) links
Transferase/signaling protein PDB id
Protein chains
318 a.a. *
132 a.a. *
SO4 ×2
_CA ×4
Waters ×177
* Residue conservation analysis
PDB id:
Name: Transferase/signaling protein
Title: X-ray structure of a dap-kinase calmodulin complex
Structure: Death-associated protein kinase 1. Chain: a. Fragment: catalytic and autoinhibitory domain, residues 1- synonym: dap kinase 1. Engineered: yes. Calmodulin. Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
2.20Å     R-factor:   0.204     R-free:   0.267
Authors: J.Kuper,I.De Diego,F.Lehmann,M.Wilmanns
Key ref: Diego et al. (2010). Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. Sci Signal, 3, ra6. PubMed id: 20103772 DOI: 10.1126/scisignal.2000552
08-Dec-09     Release date:   26-Jan-10    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P53355  (DAPK1_HUMAN) -  Death-associated protein kinase 1
1430 a.a.
318 a.a.
Protein chain
Pfam   ArchSchema ?
P62158  (CALM_HUMAN) -  Calmodulin
149 a.a.
132 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain A: E.C.  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
+ protein
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   16 terms 
  Biological process     Fc-epsilon receptor signaling pathway   47 terms 
  Biochemical function     enzyme regulator activity     22 terms  


DOI no: 10.1126/scisignal.2000552 Sci Signal 3:ra6 (2010)
PubMed id: 20103772  
Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. Diego, J.Kuper, N.Bakalova, P.Kursula, M.Wilmanns.
Death-associated protein kinase (DAPK) provides a model for calcium-bound calmodulin (CaM)-dependent protein kinases (CaMKs). Here, we report the crystal structure of the binary DAPK-CaM complex, using a construct that includes the DAPK catalytic domain and adjacent autoregulatory domain. When DAPK was in a complex with CaM, the DAPK autoregulatory domain formed a long seven-turn helix. This DAPK-CaM module interacted with the DAPK catalytic domain through two separate domain-domain interfaces, which involved the upper and the lower lobe of the catalytic domain. When bound to DAPK, CaM adopted an extended conformation, which was different from that in CaM-CaMK peptide complexes. Complementary biochemical analysis showed that the ability of DAPK to bind CaM correlated with its catalytic activity. Because many features of CaM binding are conserved in other CaMKs, our findings likely provide a generally applicable model for regulation of CaMK activity.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21287613 A.K.Wernimont, M.Amani, W.Qiu, J.C.Pizarro, J.D.Artz, Y.H.Lin, J.Lew, A.Hutchinson, and R.Hui (2011).
Structures of parasitic CDPK domains point to a common mechanism of activation.
  Proteins, 79, 803-820.
PDB codes: 3k21 3khe
21152427 M.Zimmermann, C.Atmanene, Q.Xu, L.Fouillen, A.Van Dorsselaer, D.Bonnet, C.Marsol, M.Hibert, S.Sanglier-Cianferani, C.Pigault, L.K.McNamara, D.M.Watterson, J.Haiech, and M.C.Kilhoffer (2010).
Homodimerization of the death-associated protein kinase catalytic domain: development of a new small molecule fluorescent reporter.
  PLoS One, 5, e14120.  
20668654 P.Rellos, A.C.Pike, F.H.Niesen, E.Salah, W.H.Lee, F.von Delft, and S.Knapp (2010).
Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation.
  PLoS Biol, 8, e1000426.
PDB codes: 2ux0 2v7o 2vn9 2vz6 2w2c 2wel
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