1o7b

Refined solution structure of the human TSG-6 Link module

spinqualitylabelsall models 1o7b, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1o7b is a 1 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 1tsg. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1tsg, 1o7c Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TSG6_HUMAN] Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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