[English] 日本語
![](img/lk-miru.gif)
- PDB-1du1: PEPTIDE FRAGMENT THR671-LEU690 OF THE RABBIT SKELETAL DIHYDROPYRI... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1du1 | ||||||
---|---|---|---|---|---|---|---|
Title | PEPTIDE FRAGMENT THR671-LEU690 OF THE RABBIT SKELETAL DIHYDROPYRIDINE RECEPTOR | ||||||
![]() | SKELETAL DIHYDROPYRIDINE RECEPTOR | ||||||
![]() | SIGNALING PROTEIN / DIHYDROPYRIDINE RECEPTOR / RYANODINE RECEPTOR | ||||||
Function / homology | ![]() positive regulation of muscle contraction / high voltage-gated calcium channel activity / L-type voltage-gated calcium channel complex / cellular response to caffeine / calcium ion import across plasma membrane / voltage-gated calcium channel activity / release of sequestered calcium ion into cytosol / regulation of ryanodine-sensitive calcium-release channel activity / T-tubule / muscle contraction ...positive regulation of muscle contraction / high voltage-gated calcium channel activity / L-type voltage-gated calcium channel complex / cellular response to caffeine / calcium ion import across plasma membrane / voltage-gated calcium channel activity / release of sequestered calcium ion into cytosol / regulation of ryanodine-sensitive calcium-release channel activity / 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 | ||||||
![]() | Casarotto, M. / Dulhunty, A. | ||||||
![]() | ![]() Title: 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: ![]() Title: 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. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 14.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 9.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 239 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 238.8 KB | Display | |
Data in XML | ![]() | 1.8 KB | Display | |
Data in CIF | ![]() | 1.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
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 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||
NMR details | Text: This structure was deternined using standard 2D homonuclear techniques |
-
Sample preparation
Details | Contents: 4 mM peptide, no buffer / Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 0 / pH: 5.0 / 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 |
---|
-
Processing
NMR software | Name: ![]() |
---|---|
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 |