|Entry||Database: PDB / ID: 1wq1|
|Keywords||COMPLEX (GTP-BINDING/GTPASE ACTIVATION) / RAS / GAP / SIGNAL TRANSDUCTION / GROWTH REGULATION / GTP HYDROLYSIS / TRANSITION STATE / COMPLEX (GTP-BINDING-GTPASE ACTIVATION) / COMPLEX (GTP-BINDING-GTPASE ACTIVATION) complex|
|Function / homology|
Function and homology information
regulation of RNA metabolic process / regulation of actin filament polymerization / potassium channel inhibitor activity / negative regulation of Ras protein signal transduction / negative regulation of cell adhesion / GTPase complex / positive regulation of ruffle assembly / blood vessel morphogenesis / regulation of MAP kinase activity / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane ...regulation of RNA metabolic process / regulation of actin filament polymerization / potassium channel inhibitor activity / negative regulation of Ras protein signal transduction / negative regulation of cell adhesion / GTPase complex / positive regulation of ruffle assembly / blood vessel morphogenesis / regulation of MAP kinase activity / regulation of neurotransmitter receptor localization to postsynaptic specialization membrane / positive regulation of miRNA metabolic process / T-helper 1 type immune response / positive regulation of wound healing / negative regulation of cell-matrix adhesion / negative regulation of GTPase activity / defense response to protozoan / Signaling by RAS GAP mutants / Signaling by RAS GTPase mutants / Activation of RAS in B cells / RAS signaling downstream of NF1 loss-of-function variants / positive regulation of actin cytoskeleton reorganization / mitotic cytokinesis / SOS-mediated signalling / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / SHC1 events in ERBB4 signaling / positive regulation of protein targeting to membrane / Signalling to RAS / SHC-related events triggered by IGF1R / Activated NTRK2 signals through FRS2 and FRS3 / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / ephrin receptor signaling pathway / adipose tissue development / protein-membrane adaptor activity / Estrogen-stimulated signaling through PRKCZ / vasculogenesis / SHC-mediated cascade:FGFR3 / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / MET activates RAS signaling / Signaling by FGFR4 in disease / SHC-mediated cascade:FGFR2 / positive regulation of phospholipase C activity / SHC-mediated cascade:FGFR4 / Erythropoietin activates RAS / SHC-mediated cascade:FGFR1 / Signaling by FLT3 ITD and TKD mutants / FRS-mediated FGFR3 signaling / FRS-mediated FGFR2 signaling / Tie2 Signaling / Signaling by FGFR3 in disease / FRS-mediated FGFR4 signaling / FRS-mediated FGFR1 signaling / EPHB-mediated forward signaling / G protein activity / Signaling by FGFR2 in disease / p38MAPK events / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / Signaling by FLT3 fusion proteins / Ras activation upon Ca2+ influx through NMDA receptor / EGFR Transactivation by Gastrin / FLT3 Signaling / GRB2 events in ERBB2 signaling / Signaling by FGFR1 in disease / intrinsic apoptotic signaling pathway / CD209 (DC-SIGN) signaling / GTPase activator activity / ruffle / SHC1 events in ERBB2 signaling / small monomeric GTPase / Downstream signal transduction / NCAM signaling for neurite out-growth / Constitutive Signaling by Overexpressed ERBB2 / Insulin receptor signalling cascade / phosphotyrosine residue binding / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / VEGFR2 mediated cell proliferation / positive regulation of epithelial cell proliferation / regulation of long-term neuronal synaptic plasticity / RAF activation / positive regulation of JNK cascade / FCERI mediated MAPK activation / Signaling by ERBB2 TMD/JMD mutants / animal organ morphogenesis / Signaling by high-kinase activity BRAF mutants / Constitutive Signaling by EGFRvIII / MAP2K and MAPK activation / Signaling by ERBB2 ECD mutants / Signaling by SCF-KIT / Signaling by ERBB2 KD Mutants / cellular response to gamma radiation / GTPase binding / Regulation of RAS by GAPs / GDP binding / Negative regulation of MAPK pathway / RAS processing / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF
Similarity search - Function
Ras GTPase-activating protein 1, N-terminal SH2 domain / Ras GTPase-activating protein 1 / RasGAP, SH3 domain / Ras GTPase-activating protein 1, C-terminal SH2 domain / GTPase Activation - p120GAP; domain 1 / GTPase Activation - p120gap; domain 1 / Ras GTPase-activating protein / Ras GTPase-activating protein, conserved site / Ras GTPase-activating proteins domain signature. / GTPase-activator protein for Ras-like GTPase ...Ras GTPase-activating protein 1, N-terminal SH2 domain / Ras GTPase-activating protein 1 / RasGAP, SH3 domain / Ras GTPase-activating protein 1, C-terminal SH2 domain / GTPase Activation - p120GAP; domain 1 / GTPase Activation - p120gap; domain 1 / Ras GTPase-activating protein / Ras GTPase-activating protein, conserved site / Ras GTPase-activating proteins domain signature. / GTPase-activator protein for Ras-like GTPase / Ras GTPase-activating proteins profile. / GTPase-activator protein for Ras-like GTPases / Ras GTPase-activating domain / Rho GTPase activation protein / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / Small GTPase, Ras-type / small GTPase Ras family profile. / PH domain / C2 domain superfamily / PH domain profile. / Rho (Ras homology) subfamily of Ras-like small GTPases / Pleckstrin homology domain. / Pleckstrin homology domain / Small GTPase / Ras family / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Small GTP-binding protein domain / PH-like domain superfamily / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ALUMINUM FLUORIDE / GUANOSINE-5'-DIPHOSPHATE / GTPase HRas / Ras GTPase-activating protein 1
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å|
|Authors||Scheffzek, K. / Ahmadian, M.R. / Kabsch, W. / Wiesmueller, L. / Lautwein, A. / Schmitz, F. / Wittinghofer, A.|
Journal: Science / Year: 1997
Title: The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.
Authors: Scheffzek, K. / Ahmadian, M.R. / Kabsch, W. / Wiesmuller, L. / Lautwein, A. / Schmitz, F. / Wittinghofer, A.
#1: Journal: FEBS Lett. / Year: 1997
Title: The Interaction of Ras with Gtpase-Activating Proteins
Authors: Wittinghofer, A. / Scheffzek, K. / Ahmadian, M.R.
#2: Journal: Science / Year: 1996
Title: Formation of a Transition-State Analog of the Ras Gtpase Reaction by Ras-Gdp, Tetrafluoroaluminate, and Gtpase-Activating Proteins
Authors: Mittal, R. / Ahmadian, M.R. / Goody, R.S. / Wittinghofer, A.
#3: Journal: Nature / Year: 1996
Title: Crystal Structure of the Gtpase-Activating Domain of Human P120Gap and Implications for the Interaction with Ras
Authors: Scheffzek, K. / Lautwein, A. / Kabsch, W. / Ahmadian, M.R. / Wittinghofer, A.
#4: Journal: Embo J. / Year: 1990
Title: Refined Crystal Structure of the Triphosphate Conformation of H-Ras P21 at 1.35 A Resolution: Implications for the Mechanism of GTP Hydrolysis
Authors: Pai, E.F. / Krengel, U. / Petsko, G.A. / Goody, R.S. / Kabsch, W. / Wittinghofer, A.
#5: Journal: Science / Year: 1987
Title: A Cytoplasmic Protein Stimulates Normal N-Ras P21 Gtpase, But Does not Affect Oncogenic Mutants
Authors: Trahey, M. / Mccormick, F.
#6: Journal: Cell(Cambridge,Mass.) / Year: 1986
Title: Biological and Biochemical Properties of Human Rash Genes Mutated at Codon 61
Authors: Der, C.J. / Finkel, T. / Cooper, G.M.
|Structure viewer||Molecule: |
Downloads & links
-Protein , 2 types, 2 molecules R
|#1: Protein|| |
Mass: 18875.191 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 1 - 166
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: H-RAS-1 / Organ: PLACENTA / Plasmid: PTRCGAP-334 / Gene (production host): GENE FRAGMENT OF P120GAP POSI / Production host: Escherichia coli (E. coli) / Strain (production host): CK 600 K / References: UniProt: P01112
|#2: Protein|| |
Mass: 38223.277 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 714 - 1047
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cellular location: CYTOSOL / Gene: GENE FRAGMENT OF P120GAP POSI / Organ: PLACENTA / Plasmid: PTRCGAP-334
Gene (production host): GENE FRAGMENT OF P120GAP, POSITION 2258 - 3259
Production host: Escherichia coli (E. coli) / Strain (production host): DG103 / References: UniProt: P20936
-Non-polymers , 4 types, 38 molecules
|#3: Chemical|| ChemComp-MG / |
|#4: Chemical|| ChemComp-GDP / |
|#5: Chemical|| ChemComp-AF3 / |
|#6: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.18 Å3/Da / Density % sol: 45 %|
|Crystal grow||pH: 8 / Details: SEE REF. DESCRIBING THE STRUCTURE, pH 8.|
*PLUSMethod: vapor diffusion, hanging drop / Details: used to seeding
|Components of the solutions|
|Diffraction||Mean temperature: 277 K|
|Diffraction source||Source: ROTATING ANODE / Type: ELLIOTT GX-18 / Wavelength: 1.5418|
|Detector||Type: SIEMENS / Detector: AREA DETECTOR / Date: Mar 14, 1997 / Details: FRANKS DOUBLE MIRRORS|
|Radiation||Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.5418 Å / Relative weight: 1|
|Reflection||Resolution: 2.5→30 Å / Num. obs: 15811 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Biso Wilson estimate: 41.9 Å2 / Rsym value: 0.06 / Net I/σ(I): 10|
|Reflection shell||Resolution: 2.5→2.6 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 1.1 / Rsym value: 0.35 / % possible all: 64|
*PLUSNum. measured all: 35339 / Rmerge(I) obs: 0.066
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: RAS:GPPNP (PDB ENTRY 5P21), GAP-334 (PDB ENTRY 1WER)
Resolution: 2.5→30 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
|Displacement parameters||Biso mean: 38.8 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.5→30 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 2.5→2.61 Å / Rfactor Rfree error: 0.047 / Total num. of bins used: 8 |
*PLUSName: X-PLOR / Version: 3.8 / Classification: refinement
|Refine LS restraints|
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