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- PDB-3u11: Tetramerization dynamics of the C-terminus underlies isoform-spec... -
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Basic information
Entry | Database: PDB / ID: 3u11 | ||||||
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Title | Tetramerization dynamics of the C-terminus underlies isoform-specific cAMP-gating in HCN channels | ||||||
![]() | Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 | ||||||
![]() | TRANSPORT PROTEIN | ||||||
Function / homology | ![]() voltage-gated potassium channel activity involved in SA node cell action potential depolarization / sinoatrial node development / HCN channels / HCN channel complex / regulation of cardiac muscle cell action potential involved in regulation of contraction / SA node cell action potential / membrane depolarization during SA node cell action potential / cellular response to cGMP / regulation of membrane depolarization / intracellularly cAMP-activated cation channel activity ...voltage-gated potassium channel activity involved in SA node cell action potential depolarization / sinoatrial node development / HCN channels / HCN channel complex / regulation of cardiac muscle cell action potential involved in regulation of contraction / SA node cell action potential / membrane depolarization during SA node cell action potential / cellular response to cGMP / regulation of membrane depolarization / intracellularly cAMP-activated cation channel activity / membrane depolarization during cardiac muscle cell action potential / sodium ion import across plasma membrane / blood circulation / voltage-gated sodium channel activity / voltage-gated potassium channel activity / monoatomic cation transport / regulation of heart rate by cardiac conduction / potassium ion import across plasma membrane / sodium ion transmembrane transport / regulation of cardiac muscle contraction / cAMP binding / cellular response to cAMP / potassium ion transmembrane transport / regulation of heart rate / muscle contraction / regulation of membrane potential / axon / dendrite / perinuclear region of cytoplasm / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lolicato, M. / Nardini, M. / Gazzarrini, S. / Moller, S. / Bertinetti, D. / Herberg, F.W. / Bolognesi, M. / Martin, H. / Fasolini, M. / Bertrand, J.A. ...Lolicato, M. / Nardini, M. / Gazzarrini, S. / Moller, S. / Bertinetti, D. / Herberg, F.W. / Bolognesi, M. / Martin, H. / Fasolini, M. / Bertrand, J.A. / Arrigoni, C. / Thiel, G. / Moroni, A. | ||||||
![]() | ![]() Title: Tetramerization dynamics of C-terminal domain underlies isoform-specific cAMP gating in hyperpolarization-activated cyclic nucleotide-gated channels. Authors: Lolicato, M. / Nardini, M. / Gazzarrini, S. / Moller, S. / Bertinetti, D. / Herberg, F.W. / Bolognesi, M. / Martin, H. / Fasolini, M. / Bertrand, J.A. / Arrigoni, C. / Thiel, G. / Moroni, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 100.7 KB | Display | ![]() |
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PDB format | ![]() | 76.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1006.2 KB | Display | ![]() |
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Full document | ![]() | 1018.2 KB | Display | |
Data in XML | ![]() | 20.1 KB | Display | |
Data in CIF | ![]() | 27.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3u0zC ![]() 3u10C ![]() 1q43S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 24626.133 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN (UNP RESIDUES 521-723) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.28 % |
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Crystal grow | Temperature: 278 K / Method: vapor diffusion / pH: 5 Details: 25% PEG 3350, 0.4M Sodium Acetate buffer, pH 5.0, 0.5M dibasic Ammonium phosphate, VAPOR DIFFUSION, temperature 278K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 26, 2010 |
Radiation | Monochromator: Si(111) monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97238 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→62.44 Å / Num. obs: 15615 / % possible obs: 100 % / Observed criterion σ(F): 10 / Observed criterion σ(I): 10 / Redundancy: 4.8 % / Rmerge(I) obs: 0.132 |
Reflection shell | Resolution: 2.5→2.64 Å / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1Q43 Resolution: 2.5→62.44 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.85 / SU B: 11.496 / SU ML: 0.258 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R Free: 0.347 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.282 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→62.44 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.565 Å / Total num. of bins used: 20
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