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PDBsum entry 2xs0

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protein ligands Protein-protein interface(s) links
Transcription PDB id
2xs0
Jmol
Contents
Protein chains
346 a.a.
12 a.a.
Ligands
ANP
Waters ×18
PDB id:
2xs0
Name: Transcription
Title: Linear binding motifs for jnk and for calcineurin antagonist control the nuclear shuttling of nfat4
Structure: Mitogen-activated protein kinase 8. Chain: a. Synonym: map kinase 8, mapk 8, stress-activated protein kin jnk1, jnk1, c-jun n-terminal kinase 1, jnk-46, stress-acti protein kinase 1. Engineered: yes. Mutation: yes. Nuclear factor of activated t-cells, cytoplasmic chain: b.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta plyss. Synthetic: yes. Organism_taxid: 9606
Resolution:
2.60Å     R-factor:   0.193     R-free:   0.245
Authors: T.Barkai,I.Toeoroe,A.Garai,A.Remenyi
Key ref: ..Garai et al. (2012). Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove. Sci Signal, 5, ra74. PubMed id: 23047924 DOI: 10.1126/scisignal.2003004
Date:
24-Sep-10     Release date:   28-Sep-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P45983  (MK08_HUMAN) -  Mitogen-activated protein kinase 8
Seq:
Struc:
427 a.a.
346 a.a.*
Protein chain
Pfam   ArchSchema ?
Q12968  (NFAC3_HUMAN) -  Nuclear factor of activated T-cells, cytoplasmic 3
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1075 a.a.
12 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.2.7.11.24  - Mitogen-activated protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
=
ADP
Bound ligand (Het Group name = ANP)
matches with 81.25% similarity
+ 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  

 

 
    reference    
 
 
DOI no: 10.1126/scisignal.2003004 Sci Signal 5:ra74 (2012)
PubMed id: 23047924  
 
 
Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove.
..Garai, A.Zeke, G.Gógl, I.Törő, F.Fördős, H.Blankenburg, T.Bárkai, J.Varga, A.Alexa, D.Emig, M.Albrecht, A.Reményi.
 
  ABSTRACT  
 
Mitogen-activated protein kinases (MAPKs) have a docking groove that interacts with linear "docking" motifs in binding partners. To determine the structural basis of binding specificity between MAPKs and docking motifs, we quantitatively analyzed the ability of 15 docking motifs from diverse MAPK partners to bind to c-Jun amino-terminal kinase 1 (JNK1), p38α, and extracellular signal-regulated kinase 2 (ERK2). Classical docking motifs mediated highly specific binding only to JNK1, and only those motifs with a sequence pattern distinct from the classical MAPK binding docking motif consensus differentiated between the topographically similar docking grooves of ERK and p38α. Crystal structures of four complexes of MAPKs with docking peptides, representing JNK-specific, ERK-specific, or ERK- and p38-selective binding modes, revealed that the regions located between consensus positions in the docking motifs showed conformational diversity. Although the consensus positions in the docking motifs served as anchor points that bound to common MAPK surface features and mostly contributed to docking in a nondiscriminatory fashion, the conformation of the intervening region between the anchor points mostly determined specificity. We designed peptides with tailored MAPK binding profiles by rationally changing the length and amino acid composition of intervening regions located between anchor points. These results suggest a coherent structural model for MAPK docking specificity that reveals how short linear motifs binding to a common kinase docking groove can mediate diverse interaction patterns and contribute to correct MAPK partner selection in signaling networks.