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Yorodumi- PDB-1du1: PEPTIDE FRAGMENT THR671-LEU690 OF THE RABBIT SKELETAL DIHYDROPYRI... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1du1 | ||||||
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| Title | PEPTIDE FRAGMENT THR671-LEU690 OF THE RABBIT SKELETAL DIHYDROPYRIDINE RECEPTOR | ||||||
Components | SKELETAL DIHYDROPYRIDINE RECEPTOR | ||||||
Keywords | SIGNALING PROTEIN / DIHYDROPYRIDINE RECEPTOR / RYANODINE RECEPTOR | ||||||
| Function / homology | Function and homology informationhigh voltage-gated calcium channel activity / L-type voltage-gated calcium channel complex / positive regulation of muscle contraction / cellular response to caffeine / calcium ion import across plasma membrane / regulation of ryanodine-sensitive calcium-release channel activity / voltage-gated calcium channel activity / release of sequestered calcium ion into cytosol / T-tubule / muscle contraction ...high voltage-gated calcium channel activity / L-type voltage-gated calcium channel complex / positive regulation of muscle contraction / cellular response to caffeine / calcium ion import across plasma membrane / regulation of ryanodine-sensitive calcium-release channel activity / voltage-gated calcium channel activity / release of sequestered calcium ion into cytosol / T-tubule / muscle contraction / calcium ion transmembrane transport / transmembrane transporter binding / calmodulin binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
| Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Casarotto, M. / Dulhunty, A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2000Title: A structural requirement for activation of skeletal ryanodine receptors by peptides of the dihydropyridine receptor II-III loop. Authors: Casarotto, M.G. / Gibson, F. / Pace, S.M. / Curtis, S.M. / Mulcair, M. / Dulhunty, A.F. #1: Journal: Biophys.J. / Year: 1999Title: Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12 Authors: Dulhunty, A.F. / Laver, D.R. / Gallant, E.M. / Casarotto, M.G. / Pace, S.M. / Curtis, S. / Pace, S. / Curtis, S. / Mulcair, M. | ||||||
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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 | 1du1.cif.gz | 14.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1du1.ent.gz | 9.5 KB | Display | PDB format |
| PDBx/mmJSON format | 1du1.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1du1_validation.pdf.gz | 239 KB | Display | wwPDB validaton report |
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| Full document | 1du1_full_validation.pdf.gz | 238.8 KB | Display | |
| Data in XML | 1du1_validation.xml.gz | 1.8 KB | Display | |
| Data in CIF | 1du1_validation.cif.gz | 1.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/du/1du1 ftp://data.pdbj.org/pub/pdb/validation_reports/du/1du1 | 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/peptide | Mass: 2339.764 Da / Num. of mol.: 1 / Fragment: II-III LOOP REGION, FRAGMENT THR671-LEU690 A1 / Source method: obtained synthetically Details: This peptide was chemically synthesized. The sequence of this peptide naturally occurs in rabbit (Oryctolagus cuniculus) References: UniProt: P07293 |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||
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| NMR experiment |
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| NMR details | Text: This structure was deternined using standard 2D homonuclear techniques |
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Sample preparation
| Details | Contents: 4 mM peptide, no buffer / Solvent system: 90% H2O/10% D2O |
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| Sample conditions | Ionic strength: 0 / pH: 5 / Pressure: 1 atm / Temperature: 278 K |
| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
| NMR software | Name: X-PLOR / Version: 3.1 / Developer: Brunger / Classification: refinement |
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| Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 223 restraints, 212 are NOE-derived distance constraints, 7 dihedral angle restraints and 4 distance constraints derived from hydrogen bonds |
| NMR representative | Selection criteria: closest to the average |
| NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 1 |
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