3PPE
Crystal structure of chicken VE-cadherin EC1-2
Summary for 3PPE
| Entry DOI | 10.2210/pdb3ppe/pdb |
| Descriptor | Vascular endothelial cadherin, CALCIUM ION (3 entities in total) |
| Functional Keywords | extracellular cadherin (ec) domain, beta barrel, ig-domain like, domain swapped dimer interface, calcium dependent cell-cell adhesion, cell surface, cell adhesion |
| Biological source | Gallus gallus (bantam,chickens) |
| Cellular location | Membrane; Single-pass type I membrane protein (By similarity): Q8AYD0 |
| Total number of polymer chains | 2 |
| Total formula weight | 45627.20 |
| Authors | Brasch, J.,Harrison, O.J.,Ahlsen, G.,Carnally, S.M.,Henderson, R.M.,Honig, B.,Shapiro, L.S. (deposition date: 2010-11-24, release date: 2011-02-02, Last modification date: 2023-09-06) |
| Primary citation | Brasch, J.,Harrison, O.J.,Ahlsen, G.,Carnally, S.M.,Henderson, R.M.,Honig, B.,Shapiro, L. Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin. J.Mol.Biol., 408:57-73, 2011 Cited by PubMed Abstract: Vascular endothelial cadherin (VE-cadherin), a divergent member of the type II classical cadherin family of cell adhesion proteins, mediates homophilic adhesion in the vascular endothelium. Previous investigations with a bacterially produced protein suggested that VE-cadherin forms cell surface trimers that bind between apposed cells to form hexamers. Here we report studies of mammalian-produced VE-cadherin ectodomains suggesting that, like other classical cadherins, VE-cadherin forms adhesive trans dimers between monomers located on opposing cell surfaces. Trimerization of the bacterially produced protein appears to be an artifact that arises from a lack of glycosylation. We also present the 2.1-Å-resolution crystal structure of the VE-cadherin EC1-2 adhesive region, which reveals homodimerization via the strand-swap mechanism common to classical cadherins. In common with type II cadherins, strand-swap binding involves two tryptophan anchor residues, but the adhesive interface resembles type I cadherins in that VE-cadherin does not form a large nonswapped hydrophobic surface. Thus, VE-cadherin is an outlier among classical cadherins, with characteristics of both type I and type II subfamilies. PubMed: 21269602DOI: 10.1016/j.jmb.2011.01.031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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