PDBsum entry 2oji

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Transferase PDB id
Protein chain
344 a.a. *
Waters ×101
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of erk2 in complex with n-benzyl-4-(4-(3- chlorophenyl)-1h-pyrazol-3-yl)-1h-pyrrole-2-carboxamide
Structure: Mitogen-activated protein kinase 1. Chain: a. Synonym: extracellular signal-regulated kinase 2, erk-2, mitogen-activated protein kinase 2, map kinase 2, mapk 2, p42-mapk, ert1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mapk1, erk2, prkm1. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.60Å     R-factor:   0.215     R-free:   0.267
Authors: X.Xie,M.D.Jacobs
Key ref: A.M.Aronov et al. (2007). Flipped out: structure-guided design of selective pyrazolylpyrrole ERK inhibitors. J Med Chem, 50, 1280-1287. PubMed id: 17300186 DOI: 10.1021/jm061381f
12-Jan-07     Release date:   06-Feb-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P28482  (MK01_HUMAN) -  Mitogen-activated protein kinase 1
360 a.a.
344 a.a.
Key:    PfamA 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!
  Cellular component     protein complex   21 terms 
  Biological process     viral reproduction   78 terms 
  Biochemical function     nucleotide binding     16 terms  


DOI no: 10.1021/jm061381f J Med Chem 50:1280-1287 (2007)
PubMed id: 17300186  
Flipped out: structure-guided design of selective pyrazolylpyrrole ERK inhibitors.
A.M.Aronov, C.Baker, G.W.Bemis, J.Cao, G.Chen, P.J.Ford, U.A.Germann, J.Green, M.R.Hale, M.Jacobs, J.W.Janetka, F.Maltais, G.Martinez-Botella, M.N.Namchuk, J.Straub, Q.Tang, X.Xie.
The Ras/Raf/MEK/ERK signal transduction is a key oncogenic pathway implicated in a variety of human cancers. We have identified a novel series of pyrazolylpyrroles as inhibitors of ERK. Aided by the discovery of two distinct binding modes for the pyrazolylpyrrole scaffold, structure-guided optimization culminated in the discovery of 6p, a potent and selective inhibitor of ERK.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21110380 J.L.Yap, S.Worlikar, A.D.MacKerell, P.Shapiro, and S.Fletcher (2011).
Small-molecule inhibitors of the ERK signaling pathway: Towards novel anticancer therapeutics.
  ChemMedChem, 6, 38-48.  
20818420 R.Y.Huang, M.Y.Li, M.K.Hsin, M.J.Underwood, L.T.Ma, T.S.Mok, T.D.Warner, and G.G.Chen (2011).
4-Methylnitrosamino-1-3-pyridyl-1-butanone (NNK) promotes lung cancer cell survival by stimulating thromboxane A2 and its receptor.
  Oncogene, 30, 106-116.  
20482377 S.Ramaswamy, I.Yen, S.Sideris, S.Malek, and C.E.Heise (2010).
A plate-based assay to measure cellular ERK substrate phosphorylation: utility for drug discovery of the MAPK-signaling cascade.
  Assay Drug Dev Technol, 8, 497-503.  
20045950 T.Shen, J.Lee, E.Lee, S.H.Kim, T.W.Kim, and J.Y.Cho (2010).
Cafestol, a coffee-specific diterpene, is a novel extracellular signal-regulated kinase inhibitor with AP-1-targeted inhibition of prostaglandin E2 production in lipopolysaccharide-activated macrophages.
  Biol Pharm Bull, 33, 128-132.  
19689374 K.Burkhard, S.Smith, R.Deshmukh, A.D.MacKerell, and P.Shapiro (2009).
Development of extracellular signal-regulated kinase inhibitors.
  Curr Top Med Chem, 9, 678-689.  
19261605 T.Kamenecka, J.Habel, D.Duckett, W.Chen, Y.Y.Ling, B.Frackowiak, R.Jiang, Y.Shin, X.Song, and P.Lograsso (2009).
Structure-Activity Relationships and X-ray Structures Describing the Selectivity of Aminopyrazole Inhibitors for c-Jun N-terminal Kinase 3 (JNK3) over p38.
  J Biol Chem, 284, 12853-12861.
PDB codes: 3fi2 3fi3
19356729 Y.Kim, K.Kim, H.Lee, S.Han, Y.S.Lee, J.Choe, Y.M.Kim, J.H.Hahn, J.Y.Ro, and D.Jeoung (2009).
Celastrol binds to ERK and inhibits FcepsilonRI signaling to exert an anti-allergic effect.
  Eur J Pharmacol, 612, 131-142.  
19105050 F.Chen, A.D.Mackerell, Y.Luo, and P.Shapiro (2008).
Using Caenorhabditis elegans as a model organism for evaluating extracellular signal-regulated kinase docking domain inhibitors.
  J Cell Commun Signal, 2, 81-92.  
18663490 Y.Z.Xiong, and P.Y.Chen (2008).
ONIOM DFT/PM3 calculation on the interaction between STI-571 and abelson tyrosine kinase.
  J Mol Model, 14, 1083-1086.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.