IDENTIFICATION AND CHARACTERIZATION OF A HEPARIN-BINDING SITE WITHIN THE NC1 DOMAIN OF CHICKEN COLLAGEN-XIV

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.