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Gelatin binding to the 8 F1 9 F1 module pair of human fibronectin requires site‐specific N‐glycosylation
Author(s) -
Millard Christopher J.,
Campbell Iain D.,
Pickford Andrew R.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.082
Subject(s) - fibronectin , glycosylation , chemistry , gelatin , extracellular matrix , binding site , mass spectrometry , biochemistry , chromatography
The gelatin (denatured collagen) binding domain of the extracellular matrix protein fibronectin contains three potential N‐glycosylation sites. Complete deglycosylation of this domain is known to reduce the thermal stability of the eighth type 1 ( 8 F1) module. We have conducted a site‐specific analysis of the structural and functional consequences of N‐linked glycosylation in the 8 F1 9 F1 module pair. Three glycoforms have been identified by mass spectrometry and nuclear magnetic resonance spectroscopy. Chemical shift differences between the glycoforms have revealed an intimate interaction between one N‐linked sugar and the polypeptide that is critical for gelatin binding, as shown by affinity chromatography.