› 1o0l

Solution NMR

THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY

Released:
DOI: 10.2210/pdb1o0l/pdb
PDB entry 1o0l coloured by chain, ensemble of 20 models, front view.
PDB entry 1o0l coloured by chain, ensemble of 20 models, side view.
PDB entry 1o0l coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity.
Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL
EMBO J 22 1497-507 (2003)
PMID: 12660157

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187782 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bcl-2-like protein 2 Chain: A
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 20.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92843 (Residues: 1-183; Coverage: 95%)
Gene names: BCL2L2, BCLW, KIAA0271
Sequence domains:
Structure domains: Blc2-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry torsion angle dynamics simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

37 review citations

The BCL-2 protein family: opposing activities that mediate cell death.
Youle et al. (2008)
36 more

14 mentions without citation

The deadly landscape of pro-apoptotic BCL-2 proteins in the outer mitochondrial membrane.
Luna-Vargas et al. (2016)
13 more