+Open data
-Basic information
Entry | Database: PDB / ID: 3ff7 | ||||||
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Title | Structure of NK cell receptor KLRG1 bound to E-cadherin | ||||||
Components |
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Keywords | Cell adhesion/Immune system / KLRG1-cadherin complex / Calcium / Cell adhesion / Cell junction / Cell membrane / Cleavage on pair of basic residues / Disease mutation / Glycoprotein / Membrane / Phosphoprotein / Polymorphism / Transmembrane / Alternative splicing / Lectin / Receptor / Signal-anchor / Cell adhesion-Immune system COMPLEX | ||||||
Function / homology | Function and homology information response to Gram-positive bacterium / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / pituitary gland development / gamma-catenin binding / negative regulation of axon extension / cell-cell adhesion mediated by cadherin / cellular response to indole-3-methanol / flotillin complex / Formation of definitive endoderm / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules ...response to Gram-positive bacterium / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / pituitary gland development / gamma-catenin binding / negative regulation of axon extension / cell-cell adhesion mediated by cadherin / cellular response to indole-3-methanol / flotillin complex / Formation of definitive endoderm / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / Adherens junctions interactions / catenin complex / Apoptotic cleavage of cell adhesion proteins / GTPase activating protein binding / cell-cell junction assembly / adherens junction organization / apical junction complex / ankyrin binding / negative regulation of cell-cell adhesion / cellular response to lithium ion / homophilic cell adhesion via plasma membrane adhesion molecules / lateral plasma membrane / RHO GTPases activate IQGAPs / Integrin cell surface interactions / cellular defense response / cell adhesion molecule binding / synapse assembly / InlA-mediated entry of Listeria monocytogenes into host cells / Degradation of the extracellular matrix / negative regulation of cell migration / protein tyrosine kinase binding / protein localization to plasma membrane / adherens junction / trans-Golgi network / cell morphogenesis / cytoplasmic side of plasma membrane / response to toxic substance / beta-catenin binding / cell-cell adhesion / positive regulation of protein import into nucleus / neuron projection development / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / actin cytoskeleton / lamellipodium / cell junction / signaling receptor activity / postsynapse / carbohydrate binding / regulation of gene expression / membrane => GO:0016020 / cell surface receptor signaling pathway / endosome / response to xenobiotic stimulus / cadherin binding / inflammatory response / intracellular membrane-bounded organelle / innate immune response / glutamatergic synapse / calcium ion binding / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / extracellular exosome / extracellular region / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.8 Å | ||||||
Authors | Li, Y. / Mariuzza, R.A. | ||||||
Citation | Journal: Immunity / Year: 2009 Title: Structure of natural killer cell receptor KLRG1 bound to E-cadherin reveals basis for MHC-independent missing self recognition. Authors: Li, Y. / Hofmann, M. / Wang, Q. / Teng, L. / Chlewicki, L.K. / Pircher, H. / Mariuzza, R.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ff7.cif.gz | 102 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ff7.ent.gz | 77.4 KB | Display | PDB format |
PDBx/mmJSON format | 3ff7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ff/3ff7 ftp://data.pdbj.org/pub/pdb/validation_reports/ff/3ff7 | 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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-Components
#1: Protein | Mass: 11124.637 Da / Num. of mol.: 2 / Fragment: UNP residues 155-253, Cadherin 1 domain / Mutation: C9L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CDH1, CDHE, UVO / Production host: Escherichia coli (E. coli) / References: UniProt: P12830 #2: Protein | Mass: 12972.562 Da / Num. of mol.: 2 / Fragment: UNP residues 75-186, C-type lectin domain / Mutation: C131S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KLRG1, CLEC15A, MAFA, MAFAL / Production host: Escherichia coli (E. coli) / References: UniProt: Q96E93 #3: Chemical | ChemComp-ACY / | #4: Water | ChemComp-HOH / | |
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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: 2.54 Å3/Da / Density % sol: 51.63 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 4.6 / Details: PEG4000, pH 4.6, vapor diffusion, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.502 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 7, 2008 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.502 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.65→30 Å / Num. obs: 57098 / % possible obs: 98.6 % / Redundancy: 7.3 % / Rmerge(I) obs: 0.064 / Χ2: 1.289 / Net I/σ(I): 21.542 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR | Model details: Phaser MODE: MR_AUTO
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3FF7 Resolution: 1.8→30 Å / Occupancy max: 1 / Occupancy min: 0 / σ(F): 0
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Solvent computation | Bsol: 35.739 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso max: 64.81 Å2 / Biso mean: 28.672 Å2 / Biso min: 11.36 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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Xplor file |
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