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Yorodumi- PDB-2v4z: The crystal structure of the human G-protein subunit alpha (GNAI3... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2v4z | ||||||
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Title | The crystal structure of the human G-protein subunit alpha (GNAI3) in complex with an engineered regulator of G-protein signaling type 2 domain (RGS2) | ||||||
Components |
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Keywords | CELL CYCLE / GTP HYDROLYSIS / ADP-RIBOSYLATION / NUCLEOTIDE-BINDING / LIPOPROTEIN / GTP-BINDING / PHOSPHOPROTEIN / SIGNAL TRANSDUCTION INHIBITOR / GUANINE NUCLEOTIDE BINDING PROTEIN / TRANSMEMBRANE SIGNALING / G-PROTEIN COUPLED RECEPTOR / PALMITATE / MYRISTATE / TRANSDUCER | ||||||
Function / homology | Function and homology information regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway / negative regulation of phospholipase activity / negative regulation of glycine import across plasma membrane / adenylate cyclase inhibitor activity / negative regulation of cardiac muscle hypertrophy / negative regulation of cell growth involved in cardiac muscle cell development / negative regulation of G protein-coupled receptor signaling pathway / negative regulation of adenylate cyclase activity / regulation of G protein-coupled receptor signaling pathway / relaxation of vascular associated smooth muscle ...regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway / negative regulation of phospholipase activity / negative regulation of glycine import across plasma membrane / adenylate cyclase inhibitor activity / negative regulation of cardiac muscle hypertrophy / negative regulation of cell growth involved in cardiac muscle cell development / negative regulation of G protein-coupled receptor signaling pathway / negative regulation of adenylate cyclase activity / regulation of G protein-coupled receptor signaling pathway / relaxation of vascular associated smooth muscle / GTP metabolic process / relaxation of cardiac muscle / dopamine receptor signaling pathway / beta-tubulin binding / positive regulation of macroautophagy / Adenylate cyclase inhibitory pathway / G-protein alpha-subunit binding / maternal process involved in female pregnancy / brown fat cell differentiation / positive regulation of cardiac muscle contraction / response to amphetamine / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / GTPase activator activity / negative regulation of MAP kinase activity / G protein-coupled receptor binding / G-protein beta/gamma-subunit complex binding / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / cytoplasmic side of plasma membrane / positive regulation of neuron projection development / ADP signalling through P2Y purinoceptor 12 / G alpha (z) signalling events / ADORA2B mediated anti-inflammatory cytokines production / GPER1 signaling / GDP binding / heterotrimeric G-protein complex / midbody / G alpha (i) signalling events / G alpha (s) signalling events / G alpha (q) signalling events / spermatogenesis / response to ethanol / negative regulation of translation / Extra-nuclear estrogen signaling / calmodulin binding / cell cycle / G protein-coupled receptor signaling pathway / cell division / lysosomal membrane / GTPase activity / centrosome / GTP binding / nucleolus / Golgi apparatus / mitochondrion / extracellular exosome / nucleoplasm / membrane / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Roos, A.K. / Soundararajan, M. / Pike, A.C.W. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A. / Bountra, C. / Knapp, S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2009 Title: Structural Determinants of G-Protein Alpha Subunit Selectivity by Regulator of G-Protein Signaling 2(Rgs2). Authors: Kimple, A.J. / Soundararajan, M. / Hutsell, S.Q. / Roos, A.K. / Urban, D.J. / Setola, V. / Temple, B.R. / Roth, B.L. / Knapp, S. / Willard, F.S. / Siderovski, D.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2v4z.cif.gz | 102.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2v4z.ent.gz | 75.3 KB | Display | PDB format |
PDBx/mmJSON format | 2v4z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v4/2v4z ftp://data.pdbj.org/pub/pdb/validation_reports/v4/2v4z | HTTPS FTP |
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-Related structure data
Related structure data | 2ihbS 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
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 40162.578 Da / Num. of mol.: 1 / Fragment: SUBUNIT ALPHA, RESIDUES 4-350 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC28-BSA4 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): R3-PRARE2 / References: UniProt: P08754 |
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#2: Protein | Mass: 16460.529 Da / Num. of mol.: 1 / Fragment: RGS DOMAIN, RESIDUES 71-209 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET-LIC / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): R3-PRARE2 / References: UniProt: P41220 |
-Non-polymers , 4 types, 21 molecules
#3: Chemical | ChemComp-GDP / |
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#4: Chemical | ChemComp-ALF / |
#5: Chemical | ChemComp-MG / |
#6: Water | ChemComp-HOH / |
-Details
Compound details | ENGINEERED RESIDUE IN CHAIN B, CYS 106 TO SER ENGINEERED RESIDUE IN CHAIN B, ASN 184 TO ASP ...ENGINEERED |
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Sequence details | TRIPLE MUTANT C106S, N184D, E191K |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.47 Å3/Da / Density % sol: 64.6 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: 0.1 M HEPES PH 7.5, 2 M AMMONIUM SULPHATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-E / Wavelength: 1.5418 |
Detector | Type: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE / Date: Jun 2, 2008 / Details: OSMIC MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→35.09 Å / Num. obs: 18916 / % possible obs: 99.9 % / Observed criterion σ(I): 2.3 / Redundancy: 7.2 % / Biso Wilson estimate: 67.5 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 16.2 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.86 / Mean I/σ(I) obs: 2.3 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2IHB Resolution: 2.8→33.37 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.889 / SU B: 27.265 / SU ML: 0.247 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.54 / ESU R Free: 0.317 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 44.63 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→33.37 Å
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Refine LS restraints |
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