1o7c
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(New page: 200px<br /> <applet load="1o7c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o7c" /> '''SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK ...)
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Revision as of 19:26, 29 October 2007
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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. ... [(full description)]
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
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