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This article has been peer-reviewed. It was published in Biochemical and Biophysical Research Communications 343(3):692-9, 2006. The publisher's version is available at Copyright (c) 2006 Elsevier, Inc.


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 Kd values 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.