title: Chemical shift assignments of the fibronectin III like domains 7-8 of type VII collagen.
abstract: Type VII collagen (Col7) is important for skin stability. This is underlined by the severe skin blistering phenotype in the Col7 related diseases dystrophic epidermolysis bullosa and epidermolysis bullosa acquisita (EBA). Col7 has a large N-terminal non-collagenous domain (NC1) that is followed by the triple helical collagenous domain. The NC1 domain has subdomains with homology to adhesion molecules and mediates important interactions within the extracellular matrix. An 185 amino acid long part of the NC1-subdomain termed fibronectin III like domains 7 and 8 (FNIII7-8) was investigated. Antibodies against this region are pathogenic in a mouse model of EBA and one reported missense mutations of Col7 lies within these domains. The nearly complete NMR resonance assignment of recombinant FNIII7-8 of Col7 is reported.
authors.affiliation: Institute of Chemistry, University of Lübeck, 23538, Lübeck, Germany.
authors.forename: Ulrike
authors.initials: U
authors.lastname: Hermsdorf
authors.affiliation: Institute of Chemistry, University of Lübeck, 23538, Lübeck, Germany. seeger@chemie.uni-luebeck.de.
authors.forename: Karsten
authors.initials: K
authors.lastname: Seeger
mesh_terms: D000818:Animals; D024143:Collagen Type VII / Q000737:chemistry*; D000071238:Fibronectin Type III Domain; D006863:Hydrogen-Ion Concentration; D051379:Mice; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
chemical_list: D024143:Collagen Type VII
keywords: Dystrophic epidermolysis bullosa; Epidermolysis bullosa acquisita; Extracellular matrix; Type VII collagen