6vg1 | pdb_00006vg1

xenopus protocadherin 8.1 EC1-6

spinqualitylabelsall models 6vg1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6vg1 is a 2 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: BMA, CA, CL, EDO, FUC, MAN, NA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6GLU2_XENLA Publication Abstract from PubMed Non-clustered delta1- and delta2-protocadherins, close relatives of clustered protocadherins, function in cell adhesion and motility and play essential roles in neural patterning. To understand the molecular interactions underlying these functions, we used solution biophysics to characterize binding of delta1- and delta2-protocadherins, determined crystal structures of ectodomain complexes from each family, and assessed ectodomain assembly in reconstituted intermembrane junctions by cryoelectron tomography (cryo-ET). Homophilic trans (cell-cell) interactions were preferred for all delta-protocadherins, with additional weaker heterophilic interactions observed exclusively within each subfamily. As expected, delta1- and delta2-protocadherin trans dimers formed through antiparallel EC1-EC4 interfaces, like clustered protocadherins. However, no ectodomain-mediated cis (same-cell) interactions were detectable in solution; consistent with this, cryo-ET of reconstituted junctions revealed dense assemblies lacking the characteristic order observed for clustered protocadherins. Our results define non-clustered protocadherin binding properties and their structural basis, providing a foundation for interpreting their functional roles in neural patterning. Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered delta-Protocadherins.,Harrison OJ, Brasch J, Katsamba PS, Ahlsen G, Noble AJ, Dan H, Sampogna RV, Potter CS, Carragher B, Honig B, Shapiro L Cell Rep. 2020 Feb 25;30(8):2655-2671.e7. doi: 10.1016/j.celrep.2020.02.003. PMID:32101743 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cadherin 3D structures

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