1o7c

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[[Image:1o7c.jpg|left|200px]]
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{{Structure
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|PDB= 1o7c |SIZE=350|CAPTION= <scene name='initialview01'>1o7c</scene>
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|SITE= <scene name='pdbsite=HYA:Hyaluronan-Binding+Site+(Refs+1,+3)'>HYA</scene>
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{{STRUCTURE_1o7c| PDB=1o7c | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7c OCA], [http://www.ebi.ac.uk/pdbsum/1o7c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o7c RCSB]</span>
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'''SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK MODULE IN THE PRESENCE OF A HYALURONAN OCTASACCHARIDE'''
'''SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK MODULE IN THE PRESENCE OF A HYALURONAN OCTASACCHARIDE'''
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[[Category: Pickford, A R.]]
[[Category: Pickford, A R.]]
[[Category: Teriete, P.]]
[[Category: Teriete, P.]]
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[[Category: carbohydrate-binding domain]]
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[[Category: Carbohydrate-binding domain]]
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[[Category: cell adhesion]]
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[[Category: Cell adhesion]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: hyaluronan-binding domain]]
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[[Category: Hyaluronan-binding domain]]
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[[Category: link module]]
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[[Category: Link module]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:28:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:40:55 2008''
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Revision as of 00:28, 3 May 2008

Template:STRUCTURE 1o7c

SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK MODULE IN THE PRESENCE OF A HYALURONAN OCTASACCHARIDE


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

1O7C is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Sat May 3 03:28:29 2008

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