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PDBsum entry 3k3j

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protein ligands links
Transferase PDB id
3k3j
Jmol
Contents
Protein chain
329 a.a. *
Ligands
F4C
I46
Waters ×153
* Residue conservation analysis
PDB id:
3k3j
Name: Transferase
Title: P38alpha bound to novel dfg-out compound pf-00416121
Structure: Mitogen-activated protein kinase 14. Chain: a. Synonym: mitogen-activated protein kinase p38 alpha, map ki alpha, cytokine suppressive anti-inflammatory drug-binding csaid-binding protein, csbp, max-interacting protein 2, map 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:
2.00Å     R-factor:   0.196     R-free:   0.245
Authors: S.L.Kazmirski,J.P.Dinitto
Key ref: H.Tecle et al. (2009). The design, synthesis and potential utility of fluorescence probes that target DFG-out conformation of p38alpha for high throughput screening binding assay. Chem Biol Drug Des, 74, 547-559. PubMed id: 19843080 DOI: 10.1111/j.1747-0285.2009.00884.x
Date:
02-Oct-09     Release date:   10-Nov-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.
329 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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: 10.1111/j.1747-0285.2009.00884.x Chem Biol Drug Des 74:547-559 (2009)
PubMed id: 19843080  
 
 
The design, synthesis and potential utility of fluorescence probes that target DFG-out conformation of p38alpha for high throughput screening binding assay.
H.Tecle, F.Feru, H.Liu, C.Kuhn, G.Rennie, M.Morris, J.Shao, A.C.Cheng, D.Gikunju, J.Miret, R.Coli, S.H.Xi, S.L.Clugston, S.Low, S.Kazmirski, Y.H.Ding, Q.Cao, T.L.Johnson, G.D.Deshmukh, J.P.DiNitto, J.C.Wu, J.M.English.
 
  ABSTRACT  
 
The design, synthesis and utility of fluorescence probes that bind to the DFG-out conformation of p38alpha kinase are described. Probes that demonstrate good affinity for p38alpha, have been identified and one of the probes, PF-04438255, has been successfully used in an high throughput screening (HTS) assay to identify two novel non-classical p38alpha inhibitors. In addition, a cascade activity assay was utilized to validate the selective binding of these non-classical kinase inhibitors to the unactive form of the enzyme.