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Yorodumi- PDB-4mpa: Crystal structure of NHERF1-CXCR2 signaling complex in P21 space group -
+Open data
-Basic information
Entry | Database: PDB / ID: 4mpa | ||||||
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Title | Crystal structure of NHERF1-CXCR2 signaling complex in P21 space group | ||||||
Components | Na(+)/H(+) exchange regulatory cofactor NHE-RF1, C-X-C chemokine receptor type 2 chimera | ||||||
Keywords | STRUCTURAL PROTEIN / neutrophil / inflammatory diseases | ||||||
Function / homology | Function and homology information interleukin-8-mediated signaling pathway / metanephric tubule morphogenesis / negative regulation of neutrophil apoptotic process / interleukin-8 receptor activity / mast cell granule / import across plasma membrane / channel activator activity / regulation of renal phosphate excretion / renal sodium ion transport / type 2 metabotropic glutamate receptor binding ...interleukin-8-mediated signaling pathway / metanephric tubule morphogenesis / negative regulation of neutrophil apoptotic process / interleukin-8 receptor activity / mast cell granule / import across plasma membrane / channel activator activity / regulation of renal phosphate excretion / renal sodium ion transport / type 2 metabotropic glutamate receptor binding / glutathione transport / dopamine receptor binding / renal phosphate ion absorption / gamma-aminobutyric acid transmembrane transporter activity / gamma-aminobutyric acid import / interleukin-8 binding / cerebrospinal fluid circulation / negative regulation of sodium ion transport / microvillus assembly / positive regulation of monoatomic ion transmembrane transport / C-X-C chemokine receptor activity / acute inflammatory response to antigenic stimulus / bile acid secretion / maintenance of epithelial cell apical/basal polarity / plasma membrane organization / stereocilium tip / cilium organization / intracellular phosphate ion homeostasis / gland morphogenesis / myosin II binding / phospholipase C-activating dopamine receptor signaling pathway / growth factor receptor binding / C-C chemokine receptor activity / establishment of Golgi localization / C-C chemokine binding / fibroblast migration / type 3 metabotropic glutamate receptor binding / plasma membrane protein complex / neutrophil activation / positive regulation of vascular permeability / establishment of epithelial cell apical/basal polarity / negative regulation of fibroblast migration / chloride channel regulator activity / negative regulation of platelet-derived growth factor receptor signaling pathway / positive regulation of neutrophil chemotaxis / auditory receptor cell stereocilium organization / Chemokine receptors bind chemokines / nuclear migration / regulation of protein kinase activity / dendritic cell chemotaxis / beta-2 adrenergic receptor binding / microvillus membrane / regulation of cell size / midbrain development / renal absorption / positive regulation of cardiac muscle cell apoptotic process / microvillus / transport across blood-brain barrier / negative regulation of mitotic cell cycle / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / phosphatase binding / endomembrane system / cellular defense response / positive regulation of intrinsic apoptotic signaling pathway / protein-membrane adaptor activity / sperm midpiece / ruffle / neutrophil chemotaxis / secretory granule membrane / filopodium / protein localization to plasma membrane / G protein-coupled receptor activity / cell periphery / calcium-mediated signaling / PDZ domain binding / morphogenesis of an epithelium / brush border membrane / sensory perception of sound / negative regulation of canonical Wnt signaling pathway / receptor internalization / negative regulation of ERK1 and ERK2 cascade / mitotic spindle / beta-catenin binding / Wnt signaling pathway / adenylate cyclase-activating dopamine receptor signaling pathway / positive regulation of angiogenesis / : / chemotaxis / microtubule cytoskeleton / actin cytoskeleton / phospholipase C-activating G protein-coupled receptor signaling pathway / regulation of cell shape / G alpha (i) signalling events / positive regulation of cytosolic calcium ion concentration / actin cytoskeleton organization / protein-containing complex assembly / vesicle / transmembrane transporter binding / cell surface receptor signaling pathway / inflammatory response Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.097 Å | ||||||
Authors | Jiang, Y. / Lu, G. / Wu, Y. / Brunzelle, J. / Sirinupong, N. / Li, C. / Yang, Z. | ||||||
Citation | Journal: Plos One / Year: 2013 Title: New Conformational State of NHERF1-CXCR2 Signaling Complex Captured by Crystal Lattice Trapping. Authors: Jiang, Y. / Lu, G. / Trescott, L.R. / Hou, Y. / Guan, X. / Wang, S. / Stamenkovich, A. / Brunzelle, J. / Sirinupong, N. / Li, C. / Yang, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4mpa.cif.gz | 71.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mpa.ent.gz | 54 KB | Display | PDB format |
PDBx/mmJSON format | 4mpa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/4mpa ftp://data.pdbj.org/pub/pdb/validation_reports/mp/4mpa | HTTPS FTP |
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-Related structure data
Related structure data | 4lmmC 4n6xC 4jl7S S: Starting model for refinement C: citing same article (ref.) |
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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
#1: Protein | Mass: 9860.318 Da / Num. of mol.: 1 / Fragment: SEE REMARK 999 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NHERF, NHERF1, SLC9A3R1, CXCR2 / Plasmid: pSUMO / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O14745, UniProt: P25025 |
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#2: Chemical | ChemComp-ACY / |
#3: Chemical | ChemComp-CL / |
#4: Water | ChemComp-HOH / |
Sequence details | PROTEIN IS A CHIMERA OF RESIDUES 11-95 OF PDZ DOMAIN OF NHERF1 AND RESIDUES 356-360 OF CXCR2 ...PROTEIN IS A CHIMERA OF RESIDUES 11-95 OF PDZ DOMAIN OF NHERF1 AND RESIDUES 356-360 OF CXCR2 (RESIDUE 95 OF NHERF1 AND RESIDUE 356 OF CXCR2 ARE THE SAME RESIDUE). |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.34 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.8 Details: 100 mM sodium acetate, pH 4.8, 0.2 M ammonium acetate, 24% PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97856 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 4, 2013 |
Radiation | Monochromator: diamond(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 1.097→45.5 Å / Num. all: 30032 / Num. obs: 30032 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 8.17 Å2 / Rmerge(I) obs: 0.024 / Net I/σ(I): 24.8 |
Reflection shell | Resolution: 1.097→1.16 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 4.5 / Num. unique all: 3845 / % possible all: 86 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4JL7 Resolution: 1.097→25.893 Å / SU ML: 0.07 / Cross valid method: THROUGHOUT / σ(F): 1.37 / Phase error: 14.13 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.097→25.893 Å
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Refine LS restraints |
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LS refinement shell |
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