› 2o21

Solution NMR

Solution structure of the anti-apoptotic protein Bcl-2 in complex with an acyl-sulfonamide-based ligand

Released:
DOI: 10.2210/pdb2o21/pdb
PDB entry 2o21 coloured by chain, front view.
PDB entry 2o21 coloured by chain, side view.
PDB entry 2o21 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL.
Bruncko M, Oost TK, Belli BA, Ding H, Joseph MK, Kunzer A, Martineau D, McClellan WJ, Mitten M, Ng SC, Nimmer PM, Oltersdorf T, Park CM, Petros AM, Shoemaker AR, Song X, Wang X, Wendt MD, Zhang H, Fesik SW, Rosenberg SH, Elmore SW
J Med Chem 50 641-62 (2007)
PMID: 17256834

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145305 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apoptosis regulator Bcl-2 Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 19.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10415 (Residues: 3-207; Coverage: 69%)
Gene name: BCL2
Sequence domains:
Structure domains: Blc2-like

Ligands and Environments

1 bound ligand:
Ligand 43B 1 x 43B
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

36 review citations

Reaching for high-hanging fruit in drug discovery at protein-protein interfaces.
Wells et al. (2007)
35 more

12 mentions without citation

BCL2 mutations are associated with increased risk of transformation and shortened survival in follicular lymphoma.
Correia et al. (2015)
11 more