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Yorodumi- PDB-1irp: SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1irp | ||||||
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| Title | SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN | ||||||
Components | INTERLEUKIN-1 RECEPTOR ANTAGONIST | ||||||
Keywords | CYTOKINE | ||||||
| Function / homology | Function and homology informationinterleukin-1 type I receptor antagonist activity / interleukin-1 type II receptor antagonist activity / interleukin-1, type I receptor binding / interleukin-1 receptor antagonist activity / interleukin-1, type II receptor binding / negative regulation of interleukin-1-mediated signaling pathway / negative regulation of heterotypic cell-cell adhesion / interleukin-1 receptor binding / insulin secretion / Interleukin-10 signaling ...interleukin-1 type I receptor antagonist activity / interleukin-1 type II receptor antagonist activity / interleukin-1, type I receptor binding / interleukin-1 receptor antagonist activity / interleukin-1, type II receptor binding / negative regulation of interleukin-1-mediated signaling pathway / negative regulation of heterotypic cell-cell adhesion / interleukin-1 receptor binding / insulin secretion / Interleukin-10 signaling / response to glucocorticoid / cytokine activity / acute-phase response / lipid metabolic process / Interleukin-1 signaling / immune response / inflammatory response / centrosome / extracellular space / extracellular exosome / nucleoplasm / plasma membrane / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Stockman, B.J. / Scahill, T.A. / Strakalaitis, N.A. | ||||||
Citation | Journal: FEBS Lett. / Year: 1994Title: Solution structure of human interleukin-1 receptor antagonist protein. Authors: Stockman, B.J. / Scahill, T.A. / Strakalaitis, N.A. / Brunner, D.P. / Yem, A.W. / Deibel Jr., M.R. #1: Journal: Bull.Magn.Reson. / Year: 1992Title: Interleukin-1 Receptor Antagonist Protein: Solution Secondary Structure from Noe'S and 1H Alpha and 13C Alpha Chemical Shifts Authors: Stockman, B.J. / Scahill, T.A. / Euvrard, A. / Strakalaitis, N.A. / Brunner, D.P. / Yem, A.W. / Deibel, M.R. #2: Journal: J.Biomol.NMR / Year: 1992Title: Proton, Carbon and Nitrogen Chemical Shifts Accurately Delineate Differences and Similarities in Secondary Structure between the Homologous Proteins Irap and Il-1Beta Authors: Stockman, B.J. / Scahill, T.A. / Strakalaitis, N.A. / Brunner, D.P. / Yem, A.W. / Deibel, M.R. #3: Journal: Biochemistry / Year: 1992Title: Secondary Structure and Topology of Interleukin-1 Receptor Antagonist Protein Determined by Heteronuclear Three-Dimensional NMR Spectroscopy Authors: Stockman, B.J. / Scahill, T.A. / Roy, M. / Ulrich, E.L. / Strakalaitis, N.A. / Brunner, D.P. / Yem, A.W. / Deibel, M.R. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1irp.cif.gz | 566.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1irp.ent.gz | 465.3 KB | Display | PDB format |
| PDBx/mmJSON format | 1irp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1irp_validation.pdf.gz | 356.5 KB | Display | wwPDB validaton report |
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| Full document | 1irp_full_validation.pdf.gz | 451.3 KB | Display | |
| Data in XML | 1irp_validation.xml.gz | 39.1 KB | Display | |
| Data in CIF | 1irp_validation.cif.gz | 52.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ir/1irp ftp://data.pdbj.org/pub/pdb/validation_reports/ir/1irp | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein | Mass: 17276.602 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P18510 |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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Sample preparation
| Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
| NMR software | Name: DGII / Developer: BIOSYM TECHNOLOGIES, INC. / Classification: refinement |
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| NMR ensemble | Conformers submitted total number: 12 |
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Homo sapiens (human)
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