|Entry||Database: PDB / ID: 3fay|
|Title||Crystal structure of the GAP-related domain of IQGAP1|
|Components||Ras GTPase-activating-like protein IQGAP1|
|Keywords||MEMBRANE PROTEIN / ALL ALPHA / Calmodulin-binding / Cell membrane / Membrane / Phosphoprotein|
|Function / homology|
Function and homology information
negative regulation of dephosphorylation / podocyte development / slit diaphragm / GTPase inhibitor activity / MAP-kinase scaffold activity / fibroblast migration / Nephrin family interactions / S100 protein binding / neuron projection extension / RHOV GTPase cycle ...negative regulation of dephosphorylation / podocyte development / slit diaphragm / GTPase inhibitor activity / MAP-kinase scaffold activity / fibroblast migration / Nephrin family interactions / S100 protein binding / neuron projection extension / RHOV GTPase cycle / RHOC GTPase cycle / regulation of mitotic cell cycle / cortical actin cytoskeleton / cellular response to platelet-derived growth factor stimulus / RHOQ GTPase cycle / platelet-derived growth factor receptor signaling pathway / phosphatidylinositol-3,4,5-trisphosphate binding / RHOA GTPase cycle / lateral plasma membrane / RHOU GTPase cycle / CDC42 GTPase cycle / RHO GTPases activate IQGAPs / RAC2 GTPase cycle / fibroblast growth factor receptor signaling pathway / regulation of cytokine production / positive regulation of protein kinase activity / regulation of GTPase activity / regulation of actin cytoskeleton organization / cellular response to epidermal growth factor stimulus / cellular response to calcium ion / RAC1 GTPase cycle / GTPase activator activity / ruffle / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / secretory granule membrane / actin filament / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / extrinsic component of cytoplasmic side of plasma membrane / cytoplasmic ribonucleoprotein granule / epidermal growth factor receptor signaling pathway / small GTPase 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 / protein serine/threonine kinase activator activity / Signaling by BRAF and RAF1 fusions / actin filament binding / midbody / growth cone / cell migration / microtubule / protein phosphatase binding / calmodulin binding / positive regulation of MAPK cascade / molecular adaptor activity / cadherin binding / ribonucleoprotein complex / axon / neuron projection / protein domain specific binding / focal adhesion / Neutrophil degranulation / calcium ion binding / protein kinase binding / signal transduction / extracellular exosome / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
RasGAP protein, C-terminal / RasGAP C-terminus / GTPase Activation - p120GAP; domain 1 / GTPase Activation - p120gap; domain 1 / 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 ...RasGAP protein, C-terminal / RasGAP C-terminus / GTPase Activation - p120GAP; domain 1 / GTPase Activation - p120gap; domain 1 / 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 / IQ calmodulin-binding motif / Calponin homology domain / Rho GTPase activation protein / Calponin homology (CH) domain / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / IQ motif profile. / WW/rsp5/WWP domain signature. / IQ motif, EF-hand binding site / Domain with 2 conserved Trp (W) residues / WW/rsp5/WWP domain profile. / WW domain / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Ras GTPase-activating-like protein IQGAP1
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.2 Å|
|Authors||Kurella, V.B. / Richard, J.M. / Parke, C.L. / Bellamy, H. / Worthylake, D.K.|
|Citation||Journal: J.Biol.Chem. / Year: 2009|
Title: Crystal structure of the GTPase-activating protein-related domain from IQGAP1.
Authors: Kurella, V.B. / Richard, J.M. / Parke, C.L. / Lecour, L.F. / Bellamy, H.D. / Worthylake, D.K.
|Structure viewer||Molecule: |
Downloads & links
A: Ras GTPase-activating-like protein IQGAP1
|#1: Protein|| |
Mass: 44535.023 Da / Num. of mol.: 1 / Fragment: GAP-related domain (GRD)
Source method: isolated from a genetically manipulated source
Details: ligation independent cloning vector / Source: (gene. exp.) Homo sapiens (human) / Gene: IQGAP1, KIAA0051 / Plasmid: pMCSG7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)* / References: UniProt: P46940
|#2: Chemical|| ChemComp-TRS / |
|#3: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.39 Å3/Da / Density % sol: 48.5 %|
|Crystal grow||Temperature: 277 K / Method: vapor diffusion / pH: 8.5 |
Details: 20% PEG 2000 methyl ether, 500mM MgCl2, 100mM Tris HCL, pH 8.5, VAPOR DIFFUSION, temperature 277K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: CAMD / Beamline: GCPCC / Wavelength: 0.97924, 0.97900, 0.92523|
|Detector||Type: MAR CCD 165 mm / Detector: CCD / Date: Aug 20, 2006|
|Radiation||Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Reflection||Resolution: 2.2→25 Å / Num. all: 20692 / Num. obs: 20692 / % possible obs: 86.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.6 % / Rsym value: 0.062 / Net I/σ(I): 8.9|
|Reflection shell||Resolution: 2.2→2.28 Å / Mean I/σ(I) obs: 2.1 / Rsym value: 0.242 / % possible all: 38.2|
|Refinement||Method to determine structure: MAD / Resolution: 2.2→25 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: CNS default|
|Displacement parameters||Biso mean: 47.3 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.2→25 Å|
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