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- PDB-1ujl: Solution Structure of the HERG K+ channel S5-P extracellular linker -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ujl | ||||||
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Title | Solution Structure of the HERG K+ channel S5-P extracellular linker | ||||||
![]() | Potassium voltage-gated channel subfamily H member 2 | ||||||
![]() | MEMBRANE PROTEIN / two helices / amphiphatic helix | ||||||
Function / homology | ![]() inward rectifier potassium channel complex / negative regulation of potassium ion export across plasma membrane / regulation of heart rate by hormone / Phase 3 - rapid repolarisation / voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization / membrane repolarization during action potential / membrane repolarization during ventricular cardiac muscle cell action potential / negative regulation of potassium ion transmembrane transport / membrane repolarization during cardiac muscle cell action potential / potassium ion export across plasma membrane ...inward rectifier potassium channel complex / negative regulation of potassium ion export across plasma membrane / regulation of heart rate by hormone / Phase 3 - rapid repolarisation / voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization / membrane repolarization during action potential / membrane repolarization during ventricular cardiac muscle cell action potential / negative regulation of potassium ion transmembrane transport / membrane repolarization during cardiac muscle cell action potential / potassium ion export across plasma membrane / C3HC4-type RING finger domain binding / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / regulation of membrane repolarization / membrane repolarization / positive regulation of potassium ion transmembrane transport / Voltage gated Potassium channels / inward rectifier potassium channel activity / potassium ion homeostasis / ventricular cardiac muscle cell action potential / delayed rectifier potassium channel activity / regulation of potassium ion transmembrane transport / regulation of ventricular cardiac muscle cell membrane repolarization / membrane depolarization during action potential / voltage-gated potassium channel activity / regulation of heart rate by cardiac conduction / potassium ion import across plasma membrane / cardiac muscle contraction / potassium ion transmembrane transport / voltage-gated potassium channel complex / regulation of membrane potential / cellular response to xenobiotic stimulus / scaffold protein binding / transcription cis-regulatory region binding / ubiquitin protein ligase binding / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / cell surface / protein homodimerization activity / identical protein binding / plasma membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics, distance geometry, torsion angle dynamics | ||||||
![]() | Torres, A.M. / Bansal, P.S. / Sunde, M. / Clarke, C.E. / Bursill, J.A. / Smith, D.J. / Bauskin, A. / Breit, S.N. / Campbell, T.J. / Alewood, P.F. ...Torres, A.M. / Bansal, P.S. / Sunde, M. / Clarke, C.E. / Bursill, J.A. / Smith, D.J. / Bauskin, A. / Breit, S.N. / Campbell, T.J. / Alewood, P.F. / Kuchel, P.W. / Vandenberg, J.I. | ||||||
![]() | ![]() Title: Structure of the HERG K+ channel S5P extracellular linker: role of an amphipathic alpha-helix in C-type inactivation. Authors: Torres, A.M. / Bansal, P.S. / Sunde, M. / Clarke, C.E. / Bursill, J.A. / Smith, D.J. / Bauskin, A. / Breit, S.N. / Campbell, T.J. / Alewood, P.F. / Kuchel, P.W. / Vandenberg, J.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 254.2 KB | Display | ![]() |
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PDB format | ![]() | 211 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 336.3 KB | Display | ![]() |
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Full document | ![]() | 452.1 KB | Display | |
Data in XML | ![]() | 14.3 KB | Display | |
Data in CIF | ![]() | 22.8 KB | Display | |
Arichive directory | ![]() ![]() | 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: 4589.134 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-42 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide is naturally found in Homo sapiens (human). References: UniProt: Q12809 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
NMR details | Text: The structures were determined using standard 2D homonuclear techniques |
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Sample preparation
Details | Contents: 1.4mM S5-P peptide / Solvent system: 100mM SDS, 90% H2O, 10% D2O |
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Sample conditions | Ionic strength: 0 / pH: 3.3 / Pressure: ambient / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
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: simulated annealing, molecular dynamics, distance geometry, torsion angle dynamics Software ordinal: 1 Details: The structures are based on a total of 430 restraints, 416 are NOE-derived distance constraints, 14 distance restraints from hydrogen bonds. | ||||||||||||||||||||
NMR representative | Selection criteria: used in the publication | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1600 / Conformers submitted total number: 20 |