› 2lsw

Solution NMR

Structure, sulfatide-binding properties, and inhibition of platelet aggregation by a Disabled-2-derived peptide

Released:
DOI: 10.2210/pdb2lsw/pdb
PDB entry 2lsw coloured by chain, ensemble of 20 models, front view.
PDB entry 2lsw coloured by chain, ensemble of 20 models, side view.
PDB entry 2lsw coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide.
Xiao S, Charonko JJ, Fu X, Salmanzadeh A, Davalos RV, Vlachos PP, Finkielstein CV, Capelluto DG
J Biol Chem 287 37691-702 (2012)
PMID: 22977233

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Disabled homolog 2 Chain: A
Molecule details ›
Chain: A
Length: 40 amino acids
Theoretical weight: 4.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P98082 (Residues: 24-58; Coverage: 5%)
Gene names: DAB2, DOC2
Sequence domains: Disabled homolog 2-like, sulfatide-binding motifs

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 78%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Disabled-2: A modular scaffold protein with multifaceted functions in signaling.
Finkielstein et al. (2016)
2 more

6 mentions without citation

Unfolding the Mysteries of Protein Metamorphosis.
Dishman et al. (2018)
5 more