6s4c
Crystal Structure of the vWFA2 subdomain of type VII collagenCrystal Structure of the vWFA2 subdomain of type VII collagen
Structural highlights
FunctionCO7A1_MOUSE Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen.[UniProtKB:Q02388][1] Publication Abstract from PubMedType VII collagen is an extracellular matrix protein which is important for skin stability; however, detailed information at the molecular level is scarce. The second vWFA (von-Willebrand-factor type A) domain of type VII collagen mediates important interactions, and immunization of mice induces skin blistering in certain strains. To understand vWFA2 function and the pathophysiological mechanisms leading to skin blistering, we structurally characterized this domain by X-ray crystallography and NMR-spectroscopy. Cell adhesion assays identified two new interactions: one with beta1 integrin via its RGD motif and one with laminin-332. The latter interaction was confirmed by surface plasmon resonance with a KD of about 1 mM. These data show that vWFA2 has additional functions in the extracellular matrix besides interacting with type I collagen. Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites.,Gebauer JM, Flachsenberg F, Windler C, Richer B, Baumann U, Seeger K FEBS Open Bio. 2020 Feb 7. doi: 10.1002/2211-5463.12807. PMID:32031736[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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