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Open data
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Basic information
Entry | Database: PDB / ID: 2w2x | ||||||
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Title | Complex of Rac2 and PLCg2 spPH Domain | ||||||
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![]() | SIGNALING PROTEIN/HYDROLASE / HYDROLASE / PHOSPHOLIPASE C / PHOSPHOINOSITIDES / RHO GTPASES / RAC / SH2 DOMAIN / SH3 DOMAIN / SIGNALING PROTEIN-HYDROLASE complex | ||||||
Function / homology | ![]() regulation of mast cell chemotaxis / regulation of cell-substrate adhesion / lymphocyte aggregation / follicular B cell differentiation / inositol trisphosphate biosynthetic process / regulation of calcineurin-NFAT signaling cascade / erythrocyte enucleation / positive regulation of dendritic cell cytokine production / positive regulation of mast cell proliferation / antifungal innate immune response ...regulation of mast cell chemotaxis / regulation of cell-substrate adhesion / lymphocyte aggregation / follicular B cell differentiation / inositol trisphosphate biosynthetic process / regulation of calcineurin-NFAT signaling cascade / erythrocyte enucleation / positive regulation of dendritic cell cytokine production / positive regulation of mast cell proliferation / antifungal innate immune response / phosphoinositide phospholipase C / positive regulation of interleukin-23 production / regulation of respiratory burst / phosphorylation-dependent protein binding / phospholipid catabolic process / mast cell proliferation / cellular response to lectin / regulation of neutrophil migration / regulation of mast cell degranulation / positive regulation of I-kappaB phosphorylation / response to yeast / positive regulation of cell cycle G1/S phase transition / regulation of hydrogen peroxide metabolic process / phosphatidylinositol metabolic process / Toll Like Receptor 4 (TLR4) Cascade / NADPH oxidase complex / engulfment of apoptotic cell / cell activation / respiratory burst / positive regulation of neuroinflammatory response / positive regulation of phagocytosis, engulfment / cortical cytoskeleton organization / phosphatidylinositol phospholipase C activity / Erythropoietin activates Phospholipase C gamma (PLCG) / phospholipase C activity / phosphatidylinositol biosynthetic process / macrophage activation involved in immune response / ROS and RNS production in phagocytes / programmed cell death / protein kinase regulator activity / cell projection assembly / cellular response to lipid / PCP/CE pathway / positive regulation of neutrophil chemotaxis / negative regulation of programmed cell death / motor neuron axon guidance / regulation of canonical NF-kappaB signal transduction / positive regulation of macrophage cytokine production / positive regulation of protein targeting to mitochondrion / positive regulation of reactive oxygen species biosynthetic process / positive regulation of NLRP3 inflammasome complex assembly / establishment or maintenance of cell polarity / toll-like receptor signaling pathway / small GTPase-mediated signal transduction / intracellular vesicle / regulation of T cell proliferation / positive regulation of epithelial cell migration / Dectin-2 family / Synthesis of IP3 and IP4 in the cytosol / stimulatory C-type lectin receptor signaling pathway / Fc-epsilon receptor signaling pathway / phosphatidylinositol-mediated signaling / positive regulation of receptor internalization / positive regulation of interleukin-10 production / regulation of lipid metabolic process / Generation of second messenger molecules / RHO GTPases Activate NADPH Oxidases / response to axon injury / positive regulation of type I interferon production / RAC2 GTPase cycle / Role of phospholipids in phagocytosis / positive regulation of lamellipodium assembly / positive regulation of calcium-mediated signaling / release of sequestered calcium ion into cytosol / lipopolysaccharide-mediated signaling pathway / bone resorption / regulation of cell migration / GPVI-mediated activation cascade / cellular response to calcium ion / positive regulation of interleukin-12 production / positive regulation of interleukin-2 production / phosphotyrosine residue binding / FCERI mediated Ca+2 mobilization / B cell differentiation / FCGR3A-mediated IL10 synthesis / protein tyrosine kinase binding / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / calcium-mediated signaling / regulation of actin cytoskeleton organization / actin filament organization / FCERI mediated MAPK activation / B cell receptor signaling pathway / platelet activation / CLEC7A (Dectin-1) signaling / Wnt signaling pathway / positive regulation of DNA-binding transcription factor activity / ruffle membrane / phagocytic vesicle membrane / Constitutive Signaling by Aberrant PI3K in Cancer / Signaling by CSF1 (M-CSF) in myeloid cells Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Opaleye, O. / Bunney, T.D. / Roe, S.M. / Pearl, L.H. | ||||||
![]() | ![]() Title: Structural Insights Into Formation of an Active Signaling Complex between Rac and Phospholipase C Gamma 2. Authors: Bunney, T.D. / Opaleye, O. / Roe, S.M. / Vatter, P. / Baxendale, R.W. / Walliser, C. / Everett, K.L. / Josephs, M.B. / Christow, C. / Rodrigues-Lima, F. / Gierschik, P. / Pearl, L.H. / Katan, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 243.3 KB | Display | ![]() |
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PDB format | ![]() | 190.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 27.3 KB | Display | |
Data in CIF | ![]() | 35.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2w2tC ![]() 2w2vC ![]() 2w2wC ![]() 1upqS ![]() 2ovjS C: citing same article ( S: Starting model for refinement |
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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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 20310.297 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-179 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA- ... , 2 types, 2 molecules CD
#2: Protein | Mass: 14230.834 Da / Num. of mol.: 1 / Fragment: SPLIT PH DOMAIN, RESIDUES 471-514,841-913 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P16885, phosphoinositide phospholipase C |
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#3: Protein | Mass: 14202.820 Da / Num. of mol.: 1 / Fragment: SPLIT PH DOMAIN, RESIDUES 471-514,841-913 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P16885, phosphoinositide phospholipase C |
-Non-polymers , 3 types, 41 molecules ![](data/chem/img/GSP.gif)
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#4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Compound details | ENGINEEREDSequence details | THERE IS A LEADING LINKER SEQUENCE GGGSGGS (NOT SEEN IN STRUCTURE) AND G12V MUTATION THERE IS A ...THERE IS A LEADING LINKER SEQUENCE GGGSGGS (NOT SEEN IN STRUCTURE) AND G12V MUTATION THERE IS A LEADING LINKER SEQUENCE GGGSGGS (NOT SEEN IN STRUCTURE) AND TWO SH2 DOMAINS EXCISED FROM SEQUENCE AND CHAIN REJOINED. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 54 % / Description: NONE |
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Crystal grow | Temperature: 277 K / pH: 7 Details: RAC2(2-177)GTPGS-PLCSPPH(Y495F) COMPLEX WAS CRYSTALLIZED USING A PROTEIN CONCENTRATION OF 25 MG/ML WITH PRECIPITANT (18% PEG1500, 10% GLYCEROL, 100MM SPG PH9) BY MICRO-SEEDING AT A CONSTANT TEMPERATURE OF 4C |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 12, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→70 Å / Num. obs: 29046 / % possible obs: 86.9 % / Redundancy: 3 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 1.9 / % possible all: 52.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1UPQ AND 2OVJ Resolution: 2.3→69.406 Å / SU ML: 0.47 / σ(F): 1.1 / Phase error: 40.09 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 66.445 Å2 / ksol: 0.369 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 64.77 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→69.406 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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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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