› 2lp8

Solution NMR

SOLUTION STRUCTURE OF AN APOPTOSIS ACTIVATING PHOTOSWITCHABLE BAK PEPTIDE BOUND to BCL-XL

Released:
DOI: 10.2210/pdb2lp8/pdb
PDB entry 2lp8 coloured by chain, ensemble of 21 models, front view.
PDB entry 2lp8 coloured by chain, ensemble of 21 models, side view.
PDB entry 2lp8 coloured by chain, ensemble of 21 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR solution structure of a photoswitchable apoptosis activating Bak peptide bound to Bcl-xL.
Wysoczanski P, Mart RJ, Loveridge EJ, Williams C, Whittaker SB, Crump MP, Allemann RK
J Am Chem Soc 134 7644-7 (2012)
PMID: 22515821

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170521 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bcl-2-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 21.46 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:
Bcl-2 homologous antagonist/killer Chain: B
Molecule details ›
Chain: B
Length: 18 amino acids
Theoretical weight: 1.65 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q16611 (Residues: 72-87; Coverage: 8%)
Gene names: BAK, BAK1, BCL2L7, CDN1

Ligands and Environments

1 bound ligand:
Ligand 33B 1 x 33B
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 78%
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

8 review citations

Inhibition of α-helix-mediated protein-protein interactions using designed molecules.
Azzarito et al. (2013)
7 more

1 mention without citation

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