+Open data
-Basic information
Entry | Database: PDB / ID: 4dxa | ||||||
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Title | Co-crystal structure of Rap1 in complex with KRIT1 | ||||||
Components |
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Keywords | PROTEIN BINDING / GTPase / FERM / Protein-protein interaction / GTP binding / Cytoplasmic | ||||||
Function / homology | Function and homology information Rap protein signal transduction / modification of postsynaptic structure / GTPase regulator activity / regulation of cell junction assembly / endothelium development / negative regulation of calcium ion-dependent exocytosis / positive regulation of integrin activation / negative regulation of synaptic vesicle exocytosis / calcium-ion regulated exocytosis / integrin activation ...Rap protein signal transduction / modification of postsynaptic structure / GTPase regulator activity / regulation of cell junction assembly / endothelium development / negative regulation of calcium ion-dependent exocytosis / positive regulation of integrin activation / negative regulation of synaptic vesicle exocytosis / calcium-ion regulated exocytosis / integrin activation / Rap1 signalling / negative regulation of endothelial cell migration / establishment of endothelial barrier / regulation of establishment of cell polarity / MET activates RAP1 and RAC1 / azurophil granule membrane / small GTPase-mediated signal transduction / negative regulation of endothelial cell proliferation / p130Cas linkage to MAPK signaling for integrins / GRB2:SOS provides linkage to MAPK signaling for Integrins / regulation of angiogenesis / negative regulation of endothelial cell apoptotic process / cellular response to cAMP / phosphatidylinositol-4,5-bisphosphate binding / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / lipid droplet / Integrin signaling / negative regulation of angiogenesis / cell redox homeostasis / small monomeric GTPase / G protein activity / establishment of localization in cell / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / GDP binding / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / cell-cell junction / Signaling by BRAF and RAF1 fusions / microtubule binding / angiogenesis / cell population proliferation / positive regulation of ERK1 and ERK2 cascade / cytoskeleton / GTPase activity / glutamatergic synapse / Neutrophil degranulation / protein-containing complex binding / GTP binding / protein-containing complex / extracellular space / extracellular exosome / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å | ||||||
Authors | Li, X. / Zhang, R. / Boggon, T.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2012 Title: Structural Basis for Small G Protein Effector Interaction of Ras-related Protein 1 (Rap1) and Adaptor Protein Krev Interaction Trapped 1 (KRIT1). Authors: Li, X. / Zhang, R. / Draheim, K.M. / Liu, W. / Calderwood, D.A. / Boggon, T.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4dxa.cif.gz | 217.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4dxa.ent.gz | 171.5 KB | Display | PDB format |
PDBx/mmJSON format | 4dxa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dx/4dxa ftp://data.pdbj.org/pub/pdb/validation_reports/dx/4dxa | HTTPS FTP |
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-Related structure data
Related structure data | 1c1yS S: Starting model for refinement |
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Similar 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: 19206.719 Da / Num. of mol.: 1 / Mutation: G12V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) Gene: OK/SW-cl.11, RAP1B, Ras-related protein Rap-1b (RAP1B) Plasmid: modified pET-32 / Production host: Escherichia coli (E. coli) / Strain (production host): ROSETTA / References: UniProt: P61224, small monomeric GTPase |
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#2: Protein | Mass: 37372.281 Da / Num. of mol.: 1 / Fragment: FERM domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) Gene: CCM1, Krev interaction trapped protein 1 (KRIT1), KRIT1 Plasmid: pGEX 6p-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O00522 |
#3: Chemical | ChemComp-GSP / |
#4: Chemical | ChemComp-MG / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.08 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.2M KNO3, 20% PEG3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 16, 2012 |
Radiation | Monochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→50 Å / Num. all: 37653 / Num. obs: 37653 / % possible obs: 97.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 28.6 Å2 / Rsym value: 0.083 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 3.4 % / Mean I/σ(I) obs: 2.56 / Num. unique all: 3774 / Rsym value: 0.881 / % possible all: 98.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1C1Y Resolution: 1.95→47.425 Å / Occupancy max: 1 / Occupancy min: 0.44 / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 27.61 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 31.45 Å2 / ksol: 0.297 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 190.39 Å2 / Biso mean: 41.2223 Å2 / Biso min: 18.13 Å2
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Refinement step | Cycle: LAST / Resolution: 1.95→47.425 Å
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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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