title: Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
abstract: Type VII collagen as component of anchoring fibrils plays an important role in skin architecture, however, no detailed structural information is available. Here, we describe the recombinant expression, isotope labeling, and (1)H, (15)N, (13)C chemical shift assignment of a subdomain of the murine type VII collagen - the von-Willebrand-factor-A-like domain 2 (mvWFA2). vWFA2 interacts with type I collagen and plays a central role in certain skin blistering diseases. Based on these assignments a secondary structure prediction was performed showing a properly folded protein. An interaction of mvWFA2 with its neighboring domain mFNIII-9 was characterized with NMR spectroscopy and SPR.
authors.affiliation: Institute of Chemistry, University of Luebeck, Luebeck, Germany.
authors.forename: Sarah
authors.initials: S
authors.lastname: Leineweber
authors.forename: Sarah
authors.initials: S
authors.lastname: Schönig
authors.forename: Karsten
authors.initials: K
authors.lastname: Seeger
mesh_terms: D000818:Animals; D001665:Binding Sites; D024143:Collagen Type VII / Q000737:chemistry / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D051379:Mice; D011485:Protein Binding; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D020349:Surface Plasmon Resonance; D014841:von Willebrand Factor / Q000737:chemistry / Q000378:metabolism*
chemical_list: D024143:Collagen Type VII; D014841:von Willebrand Factor