The vWFA2 domain of type VII collagen is responsible for collagen binding |
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| Authors: | Henrik Wegener Sarah Leineweber Karsten Seeger |
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| Affiliation: | 1. College of Medical Laboratory Science, Sudan University of Science and Technology, Khartoum, Sudan;2. College of Applied Medical Science, Taibah University, Almadinah Almunawwarah, Kingdom of Saudi Arabia;3. Faculty of Medicine, University of Khartoum, Sudan;4. Institute of Endemic Disease, University of Khartoum, Sudan;1. University of South Alabama, Department of Mathematics and Statistics, 411 University Blvd., Mobile, AL 36688, USA;2. Hong Kong University of Science and Technology, Department of Mathematics, Clear Water Bay, Kowloon, Hong Kong;1. Department of Biochemistry and Biotechnology, Faculty of Science, Annamalai University, Annamalainagar 608 002, Tamil Nadu, India;2. Department of Pathology, Faculty of Medicine, Annamalai University, Annamalainagar 608 002, Tamil Nadu, India;3. Division of Radiology, Dr. Kamakshi Memorial hospital, Chennai, Tamil Nadu, India |
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| Abstract: | Type VII collagen (Col7) is the major component of anchoring fibrils and very important for skin integrity. This is emphasized by the Col7 related skin blistering diseases dystrophic epidermolysis bullosa and epidermolysis bullosa acquisita. Structural data that provides insights into the interaction network of Col7 and thus providing a basis for a better understanding of the pathogenesis of the diseases is missing.We proved that the von-Willebrand-factor A like domain 2 (vWFA2) of Col7 is responsible for type I collagen binding. The interaction has a KD value of 90 μM as determined by SPR and is enthalpy driven as derived from the van’t Hoff equation. Furthermore, a hitherto unknown interaction of this domain with type IV collagen was identified. The interaction of vWFA2 with type I collagen is sensitive to the presence of magnesium ions, however, vWFA2 does not contain a magnesium binding site thus magnesium must bind to type I collagen.A lysine residue has been identified to be crucial for type I collagen binding. This allowed localization of the binding site. Mutational analysis suggests different interaction mechanisms in different species and that these interactions might be of covalent nature. |
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