6S4C
Crystal Structure of the vWFA2 subdomain of type VII collagen
Summary for 6S4C
| Entry DOI | 10.2210/pdb6s4c/pdb |
| Descriptor | Collagen alpha-1(VII) chain, MAGNESIUM ION, {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID, ... (5 entities in total) |
| Functional Keywords | vwfa, collagen vii, vwa, structural protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 21241.66 |
| Authors | Gebauer, J.M.,Flachsenberg, F.,Baumann, U.,Seeger, K. (deposition date: 2019-06-27, release date: 2020-02-19, Last modification date: 2024-01-24) |
| Primary citation | Gebauer, J.M.,Flachsenberg, F.,Windler, C.,Richer, B.,Baumann, U.,Seeger, K. Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites. Febs Open Bio, 10:580-592, 2020 Cited by PubMed Abstract: Type 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 β1 integrin via its RGD motif and one with laminin-332. The latter interaction was confirmed by surface plasmon resonance with a K of about 1 mm. These data show that vWFA2 has additional functions in the extracellular matrix besides interacting with type I collagen. PubMed: 32031736DOI: 10.1002/2211-5463.12807 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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