+Open data
-Basic information
Entry | Database: PDB / ID: 1ow0 | |||||||||
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Title | Crystal structure of human FcaRI bound to IgA1-Fc | |||||||||
Components |
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Keywords | IMMUNE SYSTEM / IgA1 / FcaRI / CD89 / antibody / Fc receptor / immunoglobulin-like domain | |||||||||
Function / homology | Function and homology information IgA receptor activity / cellular response to interferon-alpha / secretory dimeric IgA immunoglobulin complex / monomeric IgA immunoglobulin complex / secretory IgA immunoglobulin complex / Fc receptor signaling pathway / IgA binding / glomerular filtration / IgA immunoglobulin complex / neutrophil activation ...IgA receptor activity / cellular response to interferon-alpha / secretory dimeric IgA immunoglobulin complex / monomeric IgA immunoglobulin complex / secretory IgA immunoglobulin complex / Fc receptor signaling pathway / IgA binding / glomerular filtration / IgA immunoglobulin complex / neutrophil activation / positive regulation of neutrophil apoptotic process / cellular response to granulocyte macrophage colony-stimulating factor stimulus / neutrophil mediated immunity / cellular response to interleukin-6 / IgG immunoglobulin complex / immunoglobulin complex, circulating / positive regulation of respiratory burst / tertiary granule membrane / ficolin-1-rich granule membrane / Scavenging of heme from plasma / specific granule membrane / complement activation, classical pathway / antigen binding / Cell surface interactions at the vascular wall / B cell receptor signaling pathway / cellular response to type II interferon / cellular response to tumor necrosis factor / antibacterial humoral response / cellular response to lipopolysaccharide / adaptive immune response / blood microparticle / immune response / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | |||||||||
Authors | Herr, A.B. / Ballister, E.R. / Bjorkman, P.J. | |||||||||
Citation | Journal: Nature / Year: 2003 Title: Insights into IgA-mediated immune responses from the crystal structures of human Fc-alpha-RI and its complex with IgA1-Fc Authors: Herr, A.B. / Ballister, E.R. / Bjorkman, P.J. #1: Journal: J.Mol.Biol. / Year: 2003 Title: Bivalent Binding of IgA1 to FcaRI Suggests a Mechanism for Cytokine Activation of IgA Phagocytosis Authors: Herr, A.B. / White, C.L. / Milburn, C. / Wu, C. / Bjorkman, P.J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ow0.cif.gz | 165.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ow0.ent.gz | 130.1 KB | Display | PDB format |
PDBx/mmJSON format | 1ow0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ow/1ow0 ftp://data.pdbj.org/pub/pdb/validation_reports/ow/1ow0 | HTTPS FTP |
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-Related structure data
Related structure data | 1ovzSC 1dn2S 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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2 |
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3 |
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4 |
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Unit cell |
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Details | The biological assembly state is a dimer of chains A and B, which are related by 2-fold NCS. / The biological assembly state is a monomer. |
-Components
-Antibody / Protein , 2 types, 4 molecules ABCD
#1: Antibody | Mass: 23226.391 Da / Num. of mol.: 2 / Fragment: Fc region Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IGHA1 / Plasmid: pBJ5GS-MCS3 / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): Chinese hamster ovary cells / References: UniProt: P01876 #2: Protein | Mass: 23615.742 Da / Num. of mol.: 2 / Fragment: ectodomain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FCAR OR CD89 / Plasmid: pAcGP67 / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): High 5 insect cells / References: UniProt: P24071 |
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-Sugars , 6 types, 10 molecules
#3: Polysaccharide | N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D- ...N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||||
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#4: Polysaccharide | N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D- ...N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||||
#5: Polysaccharide | Source method: isolated from a genetically manipulated source #6: Polysaccharide | Source method: isolated from a genetically manipulated source #7: Polysaccharide | Source method: isolated from a genetically manipulated source #8: Sugar | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.93 Å3/Da / Density % sol: 69.3 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: magnesium sulfate heptahydrate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.95 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 4, 2002 |
Radiation | Monochromator: single crystal Si(311) bent monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→30 Å / Num. all: 27807 / Num. obs: 27262 / % possible obs: 95.8 % / Observed criterion σ(I): -3 / Redundancy: 7.7 % / Biso Wilson estimate: 73.2 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 12 |
Reflection shell | Resolution: 3.1→3.21 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.31 / Mean I/σ(I) obs: 2.4 / Num. unique all: 1998 / % possible all: 71.6 |
Reflection | *PLUS Num. obs: 27807 / Num. measured all: 213861 |
Reflection shell | *PLUS % possible obs: 71.6 % / Rmerge(I) obs: 0.31 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRIES 1DN2, 1OVZ Resolution: 3.1→29.69 Å / Rfactor Rfree error: 0.008 / Isotropic thermal model: GROUP / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 53.6167 Å2 / ksol: 0.292762 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 98.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.1→29.69 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: CONSTR | |||||||||||||||||||||||||
LS refinement shell | Resolution: 3.1→3.21 Å / Rfactor Rfree error: 0.041 / Total num. of bins used: 10
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Xplor file |
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Refinement | *PLUS Highest resolution: 3.1 Å / Lowest resolution: 30 Å / Rfactor Rwork: 0.251 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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