+Open data
-Basic information
Entry | Database: PDB / ID: 1nci | ||||||
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Title | STRUCTURAL BASIS OF CELL-CELL ADHESION BY CADHERINS | ||||||
Components | N-CADHERINCadherin-2 | ||||||
Keywords | CELL ADHESION PROTEIN / CADHERIN | ||||||
Function / homology | Function and homology information mesenchymal cell migration / regulation of oligodendrocyte progenitor proliferation / regulation of postsynaptic density protein 95 clustering / radial glial cell differentiation / neuroligin clustering involved in postsynaptic membrane assembly / positive regulation of synaptic vesicle clustering / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / Adherens junctions interactions / desmosome ...mesenchymal cell migration / regulation of oligodendrocyte progenitor proliferation / regulation of postsynaptic density protein 95 clustering / radial glial cell differentiation / neuroligin clustering involved in postsynaptic membrane assembly / positive regulation of synaptic vesicle clustering / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Post-translational protein phosphorylation / Adherens junctions interactions / desmosome / synaptic vesicle clustering / neural crest cell development / gamma-catenin binding / glial cell differentiation / cell-cell adhesion mediated by cadherin / telencephalon development / neuroepithelial cell differentiation / type B pancreatic cell development / neuronal stem cell population maintenance / alpha-catenin binding / fascia adherens / apicolateral plasma membrane / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / Myogenesis / regulation of Rho protein signal transduction / postsynaptic specialization membrane / brain morphogenesis / catenin complex / cell-cell junction assembly / adherens junction organization / blood vessel morphogenesis / regulation of myelination / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / regulation of axonogenesis / cortical actin cytoskeleton / nitric-oxide synthase binding / homophilic cell adhesion via plasma membrane adhesion molecules / plasma membrane raft / homeostasis of number of cells / intercalated disc / presynaptic active zone membrane / regulation of synaptic transmission, glutamatergic / synapse assembly / striated muscle cell differentiation / T-tubule / protein tyrosine kinase binding / protein localization to plasma membrane / adherens junction / brain development / negative regulation of canonical Wnt signaling pathway / sarcolemma / modulation of chemical synaptic transmission / cell morphogenesis / cell-cell adhesion / cerebral cortex development / beta-catenin binding / regulation of protein localization / cell-cell junction / cell migration / apical part of cell / lamellipodium / cell junction / basolateral plasma membrane / protein phosphatase binding / postsynaptic density / positive regulation of MAPK cascade / cell adhesion / neuron projection / cadherin binding / apical plasma membrane / glutamatergic synapse / synapse / calcium ion binding / protein-containing complex binding / protein kinase binding / enzyme binding / cell surface / protein-containing complex / RNA binding / membrane / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.1 Å | ||||||
Authors | Shapiro, L. / Fannon, A.M. / Kwong, P.D. / Thompson, A. / Lehmann, M.S. / Grubel, G. / Legrand, J.-F. / Als-Nielsen, J. / Colman, D.R. / Hendrickson, W.A. | ||||||
Citation | Journal: Nature / Year: 1995 Title: Structural basis of cell-cell adhesion by cadherins. Authors: Shapiro, L. / Fannon, A.M. / Kwong, P.D. / Thompson, A. / Lehmann, M.S. / Grubel, G. / Legrand, J.F. / Als-Nielsen, J. / Colman, D.R. / Hendrickson, W.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nci.cif.gz | 59.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nci.ent.gz | 43.2 KB | Display | PDB format |
PDBx/mmJSON format | 1nci.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nc/1nci ftp://data.pdbj.org/pub/pdb/validation_reports/nc/1nci | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 16 / 2: CIS PROLINE - PRO A 18 / 3: CIS PROLINE - PRO A 47 / 4: CIS PROLINE - PRO B 16 / 5: CIS PROLINE - PRO B 18 / 6: CIS PROLINE - PRO B 47 | |||||||||||||||
Components on special symmetry positions |
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Details | THE ASYMMETRIC UNIT (MOLECULES A AND B) COMPRISE A CADHERIN STRAND DIMER. AN ADHESION DIMER IS FORMED, FOR EXAMPLE, BETWEEN MOLECULE A AND THE (X + 1/2, 3/2 - Y, -1 -Z) SYMMETRY MATE OF MOLECULE B. SYMMETRY THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE. APPLIED TO RESIDUES: B 1 .. 100 ADHESION DIMER MATE OF MOLECULE A IS A SYMMETRY-MATE OF MOLECULE B, AND CAN BE GENERATED BY THE FOLLOWING TRANSFORMATION: SYMMETRY1 1 1.000000 0.000000 0.000000 37.60000 SYMMETRY2 1 0.000000 1.500000 0.000000 86.25000 SYMMETRY3 1 0.000000 0.000000 1.000000 -52.50000 |
-Components
#1: Protein | Mass: 12244.817 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PGEX-2T / Production host: Escherichia coli (E. coli) / References: UniProt: P15116 #2: Chemical | ChemComp-IUM / | #3: Water | ChemComp-HOH / | Nonpolymer details | THE MODEL INCLUDES ONE URANYL ION (UO2 2+) BOUND AT THE PUTATIVE CALCIUM BINDING SITE. | Sequence details | RESIDUE NUMBERING IS FOR THE MATURE PROTEIN. | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 46.87 % Description: 5 WAVELENGTH MAD EXPERIMENT; DATA COLLECTED NEAR URANIUM L(III) EDGE | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 19.5 ℃ / pH: 4 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.7217 - 0.7263 | |||||||||
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Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Aug 1, 1994 | |||||||||
Radiation | Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Num. obs: 33075 / % possible obs: 95.7 % / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.038 | |||||||||
Reflection | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 15 Å / Rmerge(I) obs: 0.038 |
-Processing
Software |
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Refinement | Resolution: 2.1→5 Å / σ(F): 2
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Displacement parameters | Biso mean: 17.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→5 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |