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pubmed-article:16563355pubmed:abstractTextAnchoring 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.lld:pubmed
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pubmed-article:16563355pubmed:pagination692-9lld:pubmed
pubmed-article:16563355pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:16563355pubmed:articleTitleHigh-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV.lld:pubmed
pubmed-article:16563355pubmed:affiliationDepartment of Dermatology and Cutaneous Biology, Jefferson Medical College, and Jefferson Institute of Molecular Medicine, Thomas Jefferson University, Philadelphia, PA 19107, USA.lld:pubmed
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