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PDBsum entry 2vwv

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protein ligands links
Transferase PDB id
2vwv
Jmol
Contents
Protein chain
255 a.a. *
Ligands
7X3
Waters ×138
* Residue conservation analysis
PDB id:
2vwv
Name: Transferase
Title: Ephb4 kinase domain inhibitor complex
Structure: Ephrin type-b receptor 4. Chain: a. Fragment: protein kinase domain, residues 598-899. Synonym: tyrosine-protein kinase receptor htk, tyrosine-protein kinase tyro11. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21.
Resolution:
1.90Å     R-factor:   0.241     R-free:   0.287
Authors: J.Read,C.A.Brassington,I.Green,E.J.Mccall,A.L.Valentine, J.G.Kettle,A.G.Leach
Key ref: C.Bardelle et al. (2008). Inhibitors of the tyrosine kinase EphB4. Part 1: Structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines. Bioorg Med Chem Lett, 18, 2776-2780. PubMed id: 18434142 DOI: 10.1016/j.bmcl.2008.04.015
Date:
27-Jun-08     Release date:   08-Jul-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P54760  (EPHB4_HUMAN) -  Ephrin type-B receptor 4
Seq:
Struc:
 
Seq:
Struc:
987 a.a.
255 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.1  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP
+ [protein]-L-tyrosine
= ADP
+ [protein]-L-tyrosine phosphate
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     4 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.bmcl.2008.04.015 Bioorg Med Chem Lett 18:2776-2780 (2008)
PubMed id: 18434142  
 
 
Inhibitors of the tyrosine kinase EphB4. Part 1: Structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines.
C.Bardelle, D.Cross, S.Davenport, J.G.Kettle, E.J.Ko, A.G.Leach, A.Mortlock, J.Read, N.J.Roberts, P.Robins, E.J.Williams.
 
  ABSTRACT  
 
A series of bis-anilinopyrimidines have been identified as potent inhibitors of the tyrosine kinase EphB4. Structural information from two alternative series identified from screening efforts was combined to identify the initial leads.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21441027 B.Barlaam, R.Ducray, C.Lambert-van der Brempt, P.Plé, C.Bardelle, N.Brooks, T.Coleman, D.Cross, J.G.Kettle, and J.Read (2011).
Inhibitors of the tyrosine kinase EphB4. Part 4: Discovery and optimization of a benzylic alcohol series.
  Bioorg Med Chem Lett, 21, 2207-2211.
PDB code: 2xvd
20224755 B.Mosch, B.Reissenweber, C.Neuber, and J.Pietzsch (2010).
Eph receptors and ephrin ligands: important players in angiogenesis and tumor angiogenesis.
  J Oncol, 2010, 135285.  
19942586 D.Huang, T.Zhou, K.Lafleur, C.Nevado, and A.Caflisch (2010).
Kinase selectivity potential for inhibitors targeting the ATP binding site: a network analysis.
  Bioinformatics, 26, 198-204.  
20179713 E.B.Pasquale (2010).
Eph receptors and ephrins in cancer: bidirectional signalling and beyond.
  Nat Rev Cancer, 10, 165-180.  
20803239 G.Martiny-Baron, P.Holzer, E.Billy, C.Schnell, J.Brueggen, M.Ferretti, N.Schmiedeberg, J.M.Wood, P.Furet, and P.Imbach (2010).
The small molecule specific EphB4 kinase inhibitor NVP-BHG712 inhibits VEGF driven angiogenesis.
  Angiogenesis, 13, 259-267.  
19553108 Y.Choi, F.Syeda, J.R.Walker, P.J.Finerty, D.Cuerrier, A.Wojciechowski, Q.Liu, S.Dhe-Paganon, and N.S.Gray (2009).
Discovery and structural analysis of Eph receptor tyrosine kinase inhibitors.
  Bioorg Med Chem Lett, 19, 4467-4470.  
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 code is shown on the right.