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

AbstractType 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 1H, 15N, 13C 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.Structured summary of protein interactionsmFNIII-9 and mvWFA2 bind by nuclear magnetic resonance (View interaction)mvWFA2 binds to mFNIII-9 by surface plasmon resonance (View interaction