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- PDB-1gq5: Structural Determinants of the NHERF Interaction with beta2-AR an... -
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Basic information
Entry | Database: PDB / ID: 1gq5 | ||||||
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Title | Structural Determinants of the NHERF Interaction with beta2-AR and PDGFR | ||||||
![]() | EZRIN-RADIXIN-MOESIN BINDING PHOSPHOPROTEIN-50 | ||||||
![]() | SIGNALING PROTEIN / PDZ / BETA2-ADRENERGIC RECEPTOR / PDGFR / NHERF / COMPLEX | ||||||
Function / homology | ![]() platelet activating factor receptor activity / platelet-derived growth factor receptor activity / platelet-derived growth factor beta-receptor activity / cell migration involved in coronary angiogenesis / metanephric glomerular mesangial cell proliferation involved in metanephros development / positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway / smooth muscle cell chemotaxis / import across plasma membrane / channel activator activity / regulation of renal phosphate excretion ...platelet activating factor receptor activity / platelet-derived growth factor receptor activity / platelet-derived growth factor beta-receptor activity / cell migration involved in coronary angiogenesis / metanephric glomerular mesangial cell proliferation involved in metanephros development / positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway / smooth muscle cell chemotaxis / import across plasma membrane / channel activator activity / regulation of renal phosphate excretion / renal sodium ion transport / type 2 metabotropic glutamate receptor binding / glutathione transport / metanephric glomerular capillary formation / dopamine receptor binding / renal phosphate ion absorption / gamma-aminobutyric acid transmembrane transporter activity / gamma-aminobutyric acid import / cerebrospinal fluid circulation / cell migration involved in vasculogenesis / microvillus assembly / positive regulation of monoatomic ion transmembrane transport / aorta morphogenesis / negative regulation of sodium ion transport / bile acid secretion / positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway / platelet-derived growth factor binding / maintenance of epithelial cell apical/basal polarity / plasma membrane organization / stereocilium tip / intracellular phosphate ion homeostasis / cilium organization / vascular endothelial growth factor binding / retina vasculature development in camera-type eye / cardiac myofibril assembly / gland morphogenesis / myosin II binding / phosphatidylinositol metabolic process / phospholipase C-activating dopamine receptor signaling pathway / growth factor receptor binding / establishment of Golgi localization / fibroblast migration / positive regulation of chemotaxis / Signaling by PDGF / type 3 metabotropic glutamate receptor binding / plasma membrane protein complex / establishment of epithelial cell apical/basal polarity / platelet-derived growth factor receptor binding / negative regulation of fibroblast migration / negative regulation of platelet-derived growth factor receptor signaling pathway / chloride channel regulator activity / auditory receptor cell stereocilium organization / nuclear migration / regulation of protein kinase activity / microvillus membrane / regulation of cell size / positive regulation of DNA biosynthetic process / renal absorption / positive regulation of smooth muscle cell migration / positive regulation of calcium ion import / platelet-derived growth factor receptor-beta signaling pathway / positive regulation of phosphoprotein phosphatase activity / microvillus / transport across blood-brain barrier / platelet-derived growth factor receptor signaling pathway / negative regulation of mitotic cell cycle / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / phosphatase binding / endomembrane system / : / positive regulation of calcium-mediated signaling / beta-2 adrenergic receptor binding / positive regulation of intrinsic apoptotic signaling pathway / protein-membrane adaptor activity / sperm midpiece / ruffle / Downstream signal transduction / positive regulation of mitotic nuclear division / lysosomal lumen / cell chemotaxis / filopodium / protein localization to plasma membrane / cell periphery / PDZ domain binding / morphogenesis of an epithelium / brush border membrane / regulation of actin cytoskeleton organization / sensory perception of sound / positive regulation of smooth muscle cell proliferation / positive regulation of MAP kinase activity / negative regulation of canonical Wnt signaling pathway / negative regulation of ERK1 and ERK2 cascade / receptor protein-tyrosine kinase / beta-catenin binding / Wnt signaling pathway / adenylate cyclase-activating dopamine receptor signaling pathway / peptidyl-tyrosine phosphorylation / Constitutive Signaling by Aberrant PI3K in Cancer / positive regulation of reactive oxygen species metabolic process / : Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Karthikeyan, S. / Leung, T. / Ladias, J.A.A. | ||||||
![]() | ![]() Title: Structural Determinants of the Na+/H+ Exchanger Regulatory Factor Interaction with the Beta 2 Adrenergic and Platelet-Derived Growth Factor Receptors Authors: Karthikeyan, S. / Leung, T. / Ladias, J.A.A. #1: ![]() Title: Structural Basis of the Na+/H+ Exchanger Regulatory Factor Pdz1 Interaction with the Carboxyl-Terminal Region of the Cystic Fibrosis Transmembrabe Conductance Regulator Authors: Karthikeyan, S. / Leung, T. / Ladias, J.A.A. #2: ![]() Title: Crystal Structure of the Pdz1 Domain of Human Na+/ H+ Exchanger Regulatory Factor Provides Insights Into the Mechanism of Carboxyl-Terminal Leucine Recognition by Class I Pdz Domains Authors: Karthikeyan, S. / Leung, T. / Birrane, G. / Webster, G. / Ladias, J.A.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 30.6 KB | Display | ![]() |
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PDB format | ![]() | 19.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 423.8 KB | Display | ![]() |
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Full document | ![]() | 424.9 KB | Display | |
Data in XML | ![]() | 6.6 KB | Display | |
Data in CIF | ![]() | 8.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gq4C ![]() 1i92S S: Starting model for refinement C: citing same article ( |
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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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Components
#1: Protein | Mass: 9948.382 Da / Num. of mol.: 1 / Fragment: PDZ1 DOMAIN, RESIDUES 11-94 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | RESIDUES 9-10 ARE CLONING ARTIFACTS. THE AMINO ACID RESIDUES 95-99 OF PDZ1 CORRESPOND TO THE ...RESIDUES 9-10 ARE CLONING ARTIFACTS. THE AMINO ACID RESIDUES 95-99 OF PDZ1 CORRESPOND | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 49 % |
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Crystal grow | pH: 4.6 / Details: SODIUM ACETATE, SODIUM CHLORIDE, pH 4.60 |
-Data collection
Diffraction | Mean temperature: 115 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE / Date: Jul 3, 2001 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→26.4 Å / Num. obs: 4966 / % possible obs: 95.1 % / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 11.8 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 2.9 / % possible all: 85.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1I92 Resolution: 2.2→26.4 Å / SU B: 8.267 / SU ML: 0.203 / Cross valid method: THROUGHOUT / ESU R: 0.325 / ESU R Free: 0.234
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Displacement parameters | Biso mean: 33.1 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→26.4 Å
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