1o7b

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REFINED SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK MODULE

Overview

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.

About this Structure

1O7B is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 1TSG. Full crystallographic information is available from OCA.

Reference

The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding., Blundell CD, Mahoney DJ, Almond A, DeAngelis PL, Kahmann JD, Teriete P, Pickford AR, Campbell ID, Day AJ, J Biol Chem. 2003 Dec 5;278(49):49261-70. Epub 2003 Sep 11. PMID:12972412

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