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- PDB-1kn7: Solution structure of the tandem inactivation domain (residues 1-... -

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Basic information

Entry
Database: PDB / ID: 1kn7
TitleSolution structure of the tandem inactivation domain (residues 1-75) of potassium channel RCK4 (Kv1.4)
ComponentsVOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV1.4
KeywordsMEMBRANE PROTEIN / voltage-gated potassium channel / inactivation domain / Kv1.4 / RCK4
Function / homology
Function and homology information


regulation of presynaptic membrane potential / Voltage gated Potassium channels / axon initial segment / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / voltage-gated potassium channel activity / potassium channel activity / potassium ion binding / asymmetric synapse / potassium ion transmembrane transport ...regulation of presynaptic membrane potential / Voltage gated Potassium channels / axon initial segment / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / voltage-gated potassium channel activity / potassium channel activity / potassium ion binding / asymmetric synapse / potassium ion transmembrane transport / voltage-gated potassium channel complex / monoatomic ion transmembrane transport / dendritic shaft / protein homooligomerization / potassium ion transport / presynaptic membrane / monoatomic ion channel activity / postsynaptic membrane / dendritic spine / axon / glutamatergic synapse / cell surface / membrane / plasma membrane
Similarity search - Function
Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4 / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain superfamily / Potassium channel Kv1.4 tandem inactivation domain / Potassium channel, voltage dependent, Kv1 / Potassium channel, voltage dependent, Kv / Potassium channel tetramerisation-type BTB domain / BTB/POZ domain / Broad-Complex, Tramtrack and Bric a brac ...Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4 / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain superfamily / Potassium channel Kv1.4 tandem inactivation domain / Potassium channel, voltage dependent, Kv1 / Potassium channel, voltage dependent, Kv / Potassium channel tetramerisation-type BTB domain / BTB/POZ domain / Broad-Complex, Tramtrack and Bric a brac / BTB/POZ domain / Voltage-dependent channel domain superfamily / SKP1/BTB/POZ domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Ion transport domain / Ion transport protein / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Potassium voltage-gated channel subfamily A member 4
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / simulated annealing, torsion angle dynamics
AuthorsWissmann, R. / Bildl, W. / Oliver, D. / Beyermann, M. / Kalbitzer, H.R. / Bentrop, D. / Fakler, B.
CitationJournal: J.Biol.Chem. / Year: 2003
Title: Solution Structure and Function of the "Tandem Inactivation Domain" of the Neuronal A-type Potassium Channel Kv1.4
Authors: Wissmann, R. / Bildl, W. / Oliver, D. / Beyermann, M. / Kalbitzer, H.R. / Bentrop, D. / Fakler, B.
History
DepositionDec 18, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 6, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Remark 999SEQUENCE The protein construct used in this study contains three additional residues at the N- ...SEQUENCE The protein construct used in this study contains three additional residues at the N-terminus from a thrombin cleavage site (Gly-Ser-Thr).

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Structure visualization

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Assembly

Deposited unit
A: VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV1.4


Theoretical massNumber of molelcules
Total (without water)7,8581
Polymers7,8581
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)25 / 300structures with the least restraint violations,target function
RepresentativeModel #10closest to the average

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Components

#1: Protein VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV1.4 / / RCK4


Mass: 7858.493 Da / Num. of mol.: 1
Fragment: N-terminal tandem inactivation domain (residues 1-75)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: KCNA4 / Plasmid: pET41a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P15385

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
121HNHA
1322D NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
10.8mM RCK4(1-75) U-15N; 50 mM sodium phosphate, 10 mM DTT90% H2O/10% D2O
21mM RCK4(1-75); 50 mM sodium phosphate, 10 mM DTT90% H2O/10% D2O
Sample conditionsIonic strength: 50 mM / pH: 4.4 / Pressure: ambient / Temperature: 283 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6Brukercollection
AURELIA2.7.5Brukerdata analysis
XEASY1.3.13Bartels, Xiadata analysis
DYANA1.5MUMENTHALER, GUENTERTstructure solution
DYANA1.5MUMENTHALER, GUENTERTrefinement
RefinementMethod: simulated annealing, torsion angle dynamics / Software ordinal: 1 / Details: SEE THE PRIMARY CITATION FOR STRUCTURAL STATISTICS
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the least restraint violations,target function
Conformers calculated total number: 300 / Conformers submitted total number: 25

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