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6VG1

xenopus protocadherin 8.1 EC1-6

Summary for 6VG1
Entry DOI10.2210/pdb6vg1/pdb
Descriptorprotocadherin protein, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (8 entities in total)
Functional Keywordscadherin, cell adhesion, hemophilic
Biological sourceXenopus laevis (African clawed frog)
Total number of polymer chains2
Total formula weight145299.07
Authors
Harrison, O.J.,Brasch, B.,Shapiro, L.S. (deposition date: 2020-01-07, release date: 2020-03-11, Last modification date: 2024-10-09)
Primary citationHarrison, O.J.,Brasch, J.,Katsamba, P.S.,Ahlsen, G.,Noble, A.J.,Dan, H.,Sampogna, R.V.,Potter, C.S.,Carragher, B.,Honig, B.,Shapiro, L.
Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered delta-Protocadherins.
Cell Rep, 30:2655-2671.e7, 2020
Cited by
PubMed Abstract: Non-clustered δ1- and δ2-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 δ1- and δ2-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 δ-protocadherins, with additional weaker heterophilic interactions observed exclusively within each subfamily. As expected, δ1- and δ2-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.
PubMed: 32101743
DOI: 10.1016/j.celrep.2020.02.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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数据于2024-12-25公开中

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