1O7B: Refined solution structure of the human TSG-6 Link module

The solution structure of the Link module from human TSG-6, a hyaladherin with important roles in inflammation and ovulation, has been determined in both its free and hyaluronan-bound conformations. This reveals a well defined hyaluronan-binding groove on one face of the Link module that is closed in the absence of ligand. The groove is lined with amino acids that have been implicated in mediating the interaction with hyaluronan, including two tyrosine residues that appear to form essential intermolecular hydrogen bonds and two basic residues capable of supporting ionic interactions. This is the first structure of a non-enzymic hyaladherin in its active state, and identifies a ligand-induced conformational change that is likely to be conserved across the Link module superfamily. NMR and isothermal titration calorimetry experiments with defined oligosaccharides have allowed us to infer the minimum length of hyaluronan that can be accommodated within the binding site and its polarity in the groove; these data have been used to generate a model of the complex formed between the Link module and a hyaluronan octasaccharide.
PDB ID: 1O7BDownload
MMDB ID: 25558
PDB Deposition Date: 2002/10/29
Updated in MMDB: 2003/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 1O7B: monomeric; determined by author
Molecular Components in 1O7B
Label Count Molecule
Protein (1 molecule)
Tumor Necrosis Factor-inducible Protein Tsg-6(Gene symbol: TNFAIP6)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB