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PDBsum entry 2w3l

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protein ligands Protein-protein interface(s) links
Apoptosis PDB id
2w3l
Jmol
Contents
Protein chain
141 a.a. *
Ligands
DRO ×2
Waters ×223
* Residue conservation analysis
PDB id:
2w3l
Name: Apoptosis
Title: Crystal structure of chimaeric bcl2-xl and phenyl tetrahydroisoquinoline amide complex
Structure: Apoptosis regulator bcl-2. Chain: a, b. Fragment: residues 9-33,92-206. Synonym: bcl2-xl. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.10Å     R-factor:   0.218     R-free:   0.258
Authors: J.Porter,A.Payne,B.De Candole,D.Ford,B.Hutchinson,G.Trevitt, J.Turner,C.Edwards,C.Watkins,I.Whitcombe,J.Davis, C.Stubberfield,M.Fisher,M.Lamers
Key ref: J.Porter et al. (2009). Tetrahydroisoquinoline amide substituted phenyl pyrazoles as selective Bcl-2 inhibitors. Bioorg Med Chem Lett, 19, 230-233. PubMed id: 19027294 DOI: 10.1016/j.bmcl.2008.10.113
Date:
13-Nov-08     Release date:   09-Dec-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P10415  (BCL2_HUMAN) -  Apoptosis regulator Bcl-2
Seq:
Struc:
239 a.a.
141 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     regulation of apoptotic process   2 terms 

 

 
DOI no: 10.1016/j.bmcl.2008.10.113 Bioorg Med Chem Lett 19:230-233 (2009)
PubMed id: 19027294  
 
 
Tetrahydroisoquinoline amide substituted phenyl pyrazoles as selective Bcl-2 inhibitors.
J.Porter, A.Payne, B.de Candole, D.Ford, B.Hutchinson, G.Trevitt, J.Turner, C.Edwards, C.Watkins, I.Whitcombe, J.Davis, C.Stubberfield.
 
  ABSTRACT  
 
Anti-apoptotic Bcl-2 protects cells from apoptosis by binding to pro-apoptotic members of the Bcl-2 family thereby playing a role in tumour survival in response to chemo- or radiation therapy. We describe a series of phenyl pyrazoles that have high affinity for Bcl-2 and rationalise the observed SAR by means of an X-ray crystal structure.