› 3u0z

X-ray diffraction
2.9Å resolution

Tetramerization dynamics of the C-terminus underlies isoform-specific cAMP-gating in HCN channels

Released:
DOI: 10.2210/pdb3u0z/pdb
PDB entry 3u0z coloured by chain, front view.
PDB entry 3u0z coloured by chain, side view.
PDB entry 3u0z coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Tetramerization dynamics of C-terminal domain underlies isoform-specific cAMP gating in hyperpolarization-activated cyclic nucleotide-gated channels.
Lolicato M, Nardini M, Gazzarrini S, Möller S, Bertinetti D, Herberg FW, Bolognesi M, Martin H, Fasolini M, Bertrand JA, Arrigoni C, Thiel G, Moroni A
J Biol Chem 286 44811-20 (2011)
PMID: 22006928

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131578 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 24.53 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O88704 (Residues: 390-592; Coverage: 22%)
Gene names: Bcng1, Hac2, Hcn1
Sequence domains: Cyclic nucleotide-binding domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CMP 2 x CMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I4
Unit cell:
a: 97.67Å b: 97.67Å c: 113.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.275
Expression system: Escherichia coli

Quick links

Citations

9 review citations

The Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels: from Biophysics to Pharmacology of a Unique Family of Ion Channels.
Sartiani et al. (2017)
8 more

2 mentions without citation

Structures of the Human HCN1 Hyperpolarization-Activated Channel.
Lee et al. (2017)
1 more