› 2m03

Solution NMR

Solution structure of BCL-xL determined with selective isotope labelling of I,L,V sidechains

Released:
DOI: 10.2210/pdb2m03/pdb
PDB entry 2m03 coloured by chain, ensemble of 20 models, front view.
PDB entry 2m03 coloured by chain, ensemble of 20 models, side view.
PDB entry 2m03 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis.
Follis AV, Chipuk JE, Fisher JC, Yun MK, Grace CR, Nourse A, Baran K, Ou L, Min L, White SW, Green DR, Kriwacki RW
Nat Chem Biol 9 163-8 (2013)
PMID: 23340338

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bcl-2-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 20.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07817 (Residues: 1-209; Coverage: 73%)
Gene names: BCL2L, BCL2L1, BCLX
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 46%
Refinement method: torsion angle simulated annealing, molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

29 review citations

p53 in survival, death and metabolic health: a lifeguard with a licence to kill.
Kruiswijk et al. (2015)
28 more

5 mentions without citation

The Structural Biology of Bcl-xL.
Lee et al. (2019)
4 more