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Open data
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Basic information
Entry | Database: PDB / ID: 6vg1 | ||||||||||||
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Title | xenopus protocadherin 8.1 EC1-6 | ||||||||||||
![]() | protocadherin protein | ||||||||||||
![]() | CELL ADHESION / cadherin / hemophilic | ||||||||||||
Function / homology | ![]() homophilic cell adhesion via plasma membrane adhesion molecules / membrane => GO:0016020 / calcium ion binding / plasma membrane Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Harrison, O.J. / Brasch, B. / Shapiro, L.S. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins. Authors: Oliver J Harrison / Julia Brasch / Phinikoula S Katsamba / Goran Ahlsen / Alex J Noble / Hanbin Dan / Rosemary V Sampogna / Clinton S Potter / Bridget Carragher / Barry Honig / Lawrence Shapiro / ![]() 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 ...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. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 874.6 KB | Display | ![]() |
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PDB format | ![]() | 615.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6vfpC ![]() 6vfqSC ![]() 6vfrC ![]() 6vftC ![]() 6vfuC ![]() 6vfvSC ![]() 6vfwC ![]() 6vg4C S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 70834.859 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Sugars , 2 types, 6 molecules ![](data/chem/img/MAN.gif)
#2: Polysaccharide | Source method: isolated from a genetically manipulated source #6: Sugar | ChemComp-MAN / |
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-Non-polymers , 5 types, 174 molecules ![](data/chem/img/EDO.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | ChemComp-CA / #5: Chemical | #7: Chemical | #8: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.48 Å3/Da / Density % sol: 64.62 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 10% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.135M nitrate-phosphate-sulfate mix (0.045M sodium phosphate dibasic dihydrate, 0.045M Ammonium sulfate, 0.045 M sodium nitrate; Molecular ...Details: 10% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.135M nitrate-phosphate-sulfate mix (0.045M sodium phosphate dibasic dihydrate, 0.045M Ammonium sulfate, 0.045 M sodium nitrate; Molecular Dimensions), 0.1M MES/imidazole buffer pH 6.5 with no further cryoprotection |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Apr 5, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2→40 Å / Num. obs: 59475 / % possible obs: 97.5 % / Redundancy: 4.4 % / Biso Wilson estimate: 23.21 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.13 / Net I/σ(I): 5.8 |
Reflection shell | Resolution: 2→2.03 Å / Rmerge(I) obs: 5.28 / Num. unique obs: 6132 / CC1/2: 0.37 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6VFQ, 6VFV Resolution: 2→38.27 Å / SU ML: 0.2979 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 37.1337
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Solvent computation | Shrinkage radii: 0.8 Å / VDW probe radii: 1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 68.64 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→38.27 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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