+Open data
-Basic information
Entry | Database: PDB / ID: 1g84 | ||||||
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Title | THE SOLUTION STRUCTURE OF THE C EPSILON2 DOMAIN FROM IGE | ||||||
Components | IMMUNOGLOBULIN E | ||||||
Keywords | IMMUNE SYSTEM / allergy / IgE / immunoglobulin domain / Ce2 / antibody / Fc. | ||||||
Function / homology | Function and homology information IgE B cell receptor complex / adaptive immune memory response / primary adaptive immune response / type I hypersensitivity / B cell antigen processing and presentation / Fc receptor-mediated immune complex endocytosis / eosinophil degranulation / IgE immunoglobulin complex / macrophage activation / type 2 immune response ...IgE B cell receptor complex / adaptive immune memory response / primary adaptive immune response / type I hypersensitivity / B cell antigen processing and presentation / Fc receptor-mediated immune complex endocytosis / eosinophil degranulation / IgE immunoglobulin complex / macrophage activation / type 2 immune response / Fc epsilon receptor (FCERI) signaling / antibody-dependent cellular cytotoxicity / mast cell degranulation / B cell proliferation / macrophage differentiation / Role of LAT2/NTAL/LAB on calcium mobilization / immunoglobulin complex, circulating / immunoglobulin receptor binding / FCERI mediated Ca+2 mobilization / complement activation, classical pathway / antigen binding / FCERI mediated MAPK activation / B cell receptor signaling pathway / FCERI mediated NF-kB activation / antibacterial humoral response / Interleukin-4 and Interleukin-13 signaling / adaptive immune response / inflammatory response / immune response / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / structures calculated using DYANA | ||||||
Authors | McDonnell, J.M. / Cowburn, D. / Gould, H.J. / Sutton, B.J. / Calvert, R. / Beavil, R.E. / Beavil, A.J. / Henry, A.J. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: The structure of the IgE Cepsilon2 domain and its role in stabilizing the complex with its high-affinity receptor FcepsilonRIalpha. Authors: McDonnell, J.M. / Calvert, R. / Beavil, R.L. / Beavil, A.J. / Henry, A.J. / Sutton, B.J. / Gould, H.J. / Cowburn, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g84.cif.gz | 466.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g84.ent.gz | 401.8 KB | Display | PDB format |
PDBx/mmJSON format | 1g84.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g8/1g84 ftp://data.pdbj.org/pub/pdb/validation_reports/g8/1g84 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11479.578 Da / Num. of mol.: 1 / Fragment: C EPSILON2 / Mutation: C16S, C104S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P01854 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 100mM / pH: 6 / Pressure: 1 atm / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: structures calculated using DYANA / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 1000 / Conformers submitted total number: 15 |