1O7C

Solution structure of the human TSG-6 Link module in the presence of a hyaluronan octasaccharide

Summary for 1O7C

• Entry DOI: 10.2210/pdb1o7c/pdb
• Related: 1O7B 1TSG
• NMR Information: BMRB: 6393
• Descriptor: TUMOR NECROSIS FACTOR-INDUCIBLE PROTEIN TSG-6 (1 entity in total)
• Functional Keywords: hyaluronan-binding domain, carbohydrate-binding domain, link module, cell adhesion, glycoprotein
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 10946.58

Authors

Blundell, C.D.,Teriete, P.,Kahmann, J.D.,Pickford, A.R.,Campbell, I.D.,Day, A.J. (deposition date: 2002-10-29, release date: 2003-10-23, Last modification date: 2024-11-13)

Primary citation

Blundell, C.D.,Mahoney, D.J.,Almond, A.,DeAngelis, P.L.,Kahmann, J.D.,Teriete, P.,Pickford, A.R.,Campbell, I.D.,Day, A.J.
The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding.
J. Biol. Chem., 278:49261-49270, 2003

PubMed Abstract: 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.

PubMed: 12972412
DOI: 10.1074/jbc.M309623200

Experimental method

SOLUTION NMR