High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV.
Anchoring functions of collagen VII depend on its ability to form homotypic fibrils and to bind to other macromolecules to form heterotypic complexes. Biosensor-based binding assays were employed to analyze the kinetics of the NC1 domain-mediated binding of collagen VII to laminin 5, collagen IV, and collagen I. We showed that collagen VII interacts with laminin 5 and collagen IV with a Kd value of 10(-9) M. In contrast, the NC1-mediated binding to collagen I was weak with a Kd value of 10(-6) M. Binding assays also showed that the NC1 domain utilizes the same region to bind to both laminin 5 and collagen IV. We postulate that the ability of the NC1 domains to bind with high affinities to laminin 5 and collagen IV facilitates stabilization of the structure of the basement membrane itself and that the NC1-collagen I interaction may be less important for stabilization of the dermal-epidermal junction.
Department of Dermatology and Cutaneous Biology, Jefferson Medical College, and Jefferson Institute of Molecular Medicine, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Raymond
R
Brittingham
Jouni
J
Uitto
Andrzej
A
Fertala
D001665:Binding Sites; D015374:Biosensing Techniques; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D024141:Collagen Type IV / Q000378:metabolism*; D024143:Collagen Type VII / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D017434:Protein Structure, Tertiary; D000097794:Kalinin
D015815:Cell Adhesion Molecules; D024141:Collagen Type IV; D024143:Collagen Type VII; D000097794:Kalinin