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.
FEBS Lett. 2011 May 9;
Authors: Leineweber S, Schönig S, Seeger K
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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: mFNIII-9 and mvWFA2bind by nuclear magnetic resonance (View interaction) mvWFA2binds to mFNIII-9 by surface plasmon resonance (View interaction).
PMID: 21570975 [PubMed - as supplied by publisher]
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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.
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