PDBsum entry 4ic8

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protein Protein-protein interface(s) links
Transferase PDB id
Protein chain
325 a.a.
PDB id:
Name: Transferase
Title: Crystal structure of the apo erk5 kinase domain
Structure: Mitogen-activated protein kinase 7. Chain: a, b. Synonym: map kinase 7, mapk 7, big map kinase 1, bmk-1, ext signal-regulated kinase 5, erk-5. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mapk7, bmk1, erk5, prkm7. Expressed in: escherichia coli. Expression_system_taxid: 562
2.80Å     R-factor:   0.263     R-free:   0.290
Authors: G.Gogl,A.Remenyi
Key ref: G.Glatz et al. (2013). Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module. J Biol Chem, 288, 8596-8609. PubMed id: 23382384 DOI: 10.1074/jbc.M113.452235
10-Dec-12     Release date:   13-Feb-13    
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Protein chains
Pfam   ArchSchema ?
Q13164  (MK07_HUMAN) -  Mitogen-activated protein kinase 7
816 a.a.
325 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Mitogen-activated 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!
  Biological process     protein phosphorylation   1 term 
  Biochemical function     transferase activity, transferring phosphorus-containing groups     5 terms  


DOI no: 10.1074/jbc.M113.452235 J Biol Chem 288:8596-8609 (2013)
PubMed id: 23382384  
Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module.
G.Glatz, G.Gógl, A.Alexa, A.Reményi.
Mitogen-activated protein kinase (MAPK) activation depends on a linear binding motif found in all MAPK kinases (MKK). In addition, the PB1 (Phox and Bem1) domain of MKK5 is required for extracellular signal regulated kinase 5 (ERK5) activation. We present the crystal structure of ERK5 in complex with an MKK5 construct comprised of the PB1 domain and the linear binding motif. We show that ERK5 has distinct protein-protein interaction surfaces compared with ERK2, which is the closest ERK5 paralog. The two MAPKs have characteristically different physiological functions and their distinct protein-protein interaction surface topography enables them to bind different sets of activators and substrates. Structural and biochemical characterization revealed that the MKK5 PB1 domain cooperates with the MAPK binding linear motif to achieve substrate specific binding, and it also enables co-recruitment of the upstream activating enzyme and the downstream substrate into one signaling competent complex. Studies on present day MAPKs and MKKs hint on the way protein kinase networks may evolve. In particular, they suggest how paralogous enzymes with similar catalytic properties could acquire novel signaling roles by merely changing the way they make physical links to other proteins.