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The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding

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The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding. / Blundell, C.; Mahoney, D.; Almond, A.; DeAngelis, P.; Kahmann, J.; Teriete, P.; Pickford, Andy; Campbell, I.; Day, A.

In: The Journal of Biological Chemistry, Vol. 278, No. 49, 2003, p. 49261-49270.

Research output: Contribution to journalArticlepeer-review

Harvard

Blundell, C, Mahoney, D, Almond, A, DeAngelis, P, Kahmann, J, Teriete, P, Pickford, A, Campbell, I & Day, A 2003, 'The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding', The Journal of Biological Chemistry, vol. 278, no. 49, pp. 49261-49270. https://doi.org/10.1074/jbc.M309623200

APA

Blundell, C., Mahoney, D., Almond, A., DeAngelis, P., Kahmann, J., Teriete, P., Pickford, A., Campbell, I., & Day, A. (2003). The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding. The Journal of Biological Chemistry, 278(49), 49261-49270. https://doi.org/10.1074/jbc.M309623200

Vancouver

Blundell C, Mahoney D, Almond A, DeAngelis P, Kahmann J, Teriete P et al. The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding. The Journal of Biological Chemistry. 2003;278(49):49261-49270. https://doi.org/10.1074/jbc.M309623200

Author

Blundell, C. ; Mahoney, D. ; Almond, A. ; DeAngelis, P. ; Kahmann, J. ; Teriete, P. ; Pickford, Andy ; Campbell, I. ; Day, A. / The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding. In: The Journal of Biological Chemistry. 2003 ; Vol. 278, No. 49. pp. 49261-49270.

Bibtex

@article{bf4751b4560e4325929c7166b2f6b860,
title = "The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding",
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.",
author = "C. Blundell and D. Mahoney and A. Almond and P. DeAngelis and J. Kahmann and P. Teriete and Andy Pickford and I. Campbell and A. Day",
year = "2003",
doi = "10.1074/jbc.M309623200",
language = "English",
volume = "278",
pages = "49261--49270",
journal = "The Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "49",

}

RIS

TY - JOUR

T1 - The Link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding

AU - Blundell, C.

AU - Mahoney, D.

AU - Almond, A.

AU - DeAngelis, P.

AU - Kahmann, J.

AU - Teriete, P.

AU - Pickford, Andy

AU - Campbell, I.

AU - Day, A.

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

U2 - 10.1074/jbc.M309623200

DO - 10.1074/jbc.M309623200

M3 - Article

VL - 278

SP - 49261

EP - 49270

JO - The Journal of Biological Chemistry

JF - The Journal of Biological Chemistry

SN - 0021-9258

IS - 49

ER -

ID: 156039