6VFR
Crystal structure of human protocadherin 18 EC1-EC4
Summary for 6VFR
| Entry DOI | 10.2210/pdb6vfr/pdb |
| Descriptor | Protocadherin-18, 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, alpha-L-fucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | cadherin extracellular region, non-clustered delta2 family protocadherin, homophilic adhesion/recognition calcium-dependent adhesion molecule, cell adhesion |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 102371.23 |
| Authors | Harrison, O.J.,Brasch, J.,Shapiro, L. (deposition date: 2020-01-06, release date: 2020-03-11, Last modification date: 2023-10-11) |
| Primary citation | Harrison, 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: 32101743DOI: 10.1016/j.celrep.2020.02.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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