C. Girylozinguez et al., IDENTIFICATION AND CHARACTERIZATION OF A HEPARIN-BINDING SITE WITHIN THE NC1 DOMAIN OF CHICKEN COLLAGEN-XIV, Matrix biology, 17(2), 1998, pp. 145-149
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 i
nteraction 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 seq
uence tend to fold into alpha-helix. These fragments interact specific
ally 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.