› 2i83

Solution NMR

hyaluronan-binding domain of CD44 in its ligand-bound form

Released:
DOI: 10.2210/pdb2i83/pdb
PDB entry 2i83 coloured by chain, ensemble of 20 models, front view.
PDB entry 2i83 coloured by chain, ensemble of 20 models, side view.
PDB entry 2i83 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR.
Takeda M, Ogino S, Umemoto R, Sakakura M, Kajiwara M, Sugahara KN, Hayasaka H, Miyasaka M, Terasawa H, Shimada I
J Biol Chem 281 40089-95 (2006)
PMID: 17085435

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-147592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CD44 antigen Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 17.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P16070 (Residues: 19-178; Coverage: 22%)
Gene names: CD44, LHR, MDU2, MDU3, MIC4
Sequence domains: Extracellular link domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

Functional dynamics of proteins revealed by solution NMR.
Osawa et al. (2012)
8 more

9 mentions without citation

CD44 receptor unfolding enhances binding by freeing basic amino acids to contact carbohydrate ligand.
Favreau et al. (2013)
8 more