1O7C

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

1O7C の概要

• エントリーDOI: 10.2210/pdb1o7c/pdb
• 関連するPDBエントリー: 1O7B 1TSG
• NMR情報: BMRB: 6393
• 分子名称: TUMOR NECROSIS FACTOR-INDUCIBLE PROTEIN TSG-6 (1 entity in total)
• 機能のキーワード: hyaluronan-binding domain, carbohydrate-binding domain, link module, cell adhesion, glycoprotein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10946.58

構造登録者

Blundell, C.D.,Teriete, P.,Kahmann, J.D.,Pickford, A.R.,Campbell, I.D.,Day, A.J. (登録日: 2002-10-29, 公開日: 2003-10-23, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

SOLUTION NMR