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Identification and characterization of a heparin binding site within the NC1 domain of chicken collagen XIV.

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Giry-Lozinguez, C. | Aubert-Foucher, E. | Penin, F. | Deleage, G. | Dublet, B. | Vanderrest, M.

Edité par CCSD ; Elsevier -

International audience. Collagen XIV is known to bind to the dermatan sulfate chain of decorin and to the heparan sulfate chain of perlecan. To study its possible interaction with glycosaminoglycans, the NC1 domain of chicken collagen XIV was overproduced in E. coli. Purified NC1*(6-119)* appears poorly organized (the asterisks indicate the presence of extension sequences), but V8-protease generated fragments containing the 84-108 basic sequence tend to fold into alpha-helix. These fragments interact specifically with heparin, which induces an alpha-helical fold with a maximum effect for equimolar heparin/peptide ratio. These data demonstrate the existence of a glycosaminoglycan binding site in NC1.

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