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PDBsum entry 3gi3

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protein ligands links
Transferase PDB id
3gi3
Jmol
Contents
Protein chain
330 a.a. *
Ligands
B10
Waters ×179
* Residue conservation analysis
PDB id:
3gi3
Name: Transferase
Title: Crystal structure of a n-phenyl-n'-naphthylurea analog in complex with p38 map kinase
Structure: Mitogen-activated protein kinase 14. Chain: a. Synonym: mitogen-activated protein kinase p38 alpha, map kinase p38 alpha, cytokine suppressive anti-inflammatory drug-binding protein, csaid-binding protein, csbp, max- interacting protein 2, map kinase mxi2, sapk2a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mapk14, csbp, csbp1, csbp2, cspb1, mxi2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å     R-factor:   0.230     R-free:   0.289
Authors: K.C.Qian
Key ref: P.F.Cirillo et al. (2009). Discovery and characterization of the N-phenyl-N'-naphthylurea class of p38 kinase inhibitors. Bioorg Med Chem Lett, 19, 2386-2391. PubMed id: 19356929 DOI: 10.1016/j.bmcl.2009.03.104
Date:
05-Mar-09     Release date:   20-Oct-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q16539  (MK14_HUMAN) -  Mitogen-activated protein kinase 14
Seq:
Struc:
360 a.a.
330 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.24  - Mitogen-activated protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cell   8 terms 
  Biological process     intracellular signal transduction   71 terms 
  Biochemical function     nucleotide binding     11 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.bmcl.2009.03.104 Bioorg Med Chem Lett 19:2386-2391 (2009)
PubMed id: 19356929  
 
 
Discovery and characterization of the N-phenyl-N'-naphthylurea class of p38 kinase inhibitors.
P.F.Cirillo, E.R.Hickey, N.Moss, S.Breitfelder, R.Betageri, T.Fadra, F.Gaenzler, T.Gilmore, D.R.Goldberg, V.Kamhi, T.Kirrane, R.R.Kroe, J.Madwed, M.Moriak, M.Netherton, C.A.Pargellis, U.R.Patel, K.C.Qian, R.Sharma, S.Sun, A.Swinamer, C.Torcellini, H.Takahashi, M.Tsang, Z.Xiong.
 
  ABSTRACT  
 
An effort aimed at exploring structural diversity in the N-pyrazole-N'-naphthylurea class of p38 kinase inhibitors led to the synthesis and characterization of N-phenyl-N'-naphthylureas. Examples of these compounds displayed excellent inhibition of TNF-alpha production in vitro, as well as efficacy in a mouse model of lipopolysaccharide induced endotoxemia. In addition, perspective is provided on the role of a sulfonamide functionality in defining inhibitor potency.