› 2mng

Solution NMR

Apo Structure of human HCN4 CNBD solved by NMR

Released:
DOI: 10.2210/pdb2mng/pdb
PDB entry 2mng coloured by chain, ensemble of 10 models, front view.
PDB entry 2mng coloured by chain, ensemble of 10 models, side view.
PDB entry 2mng coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
A mechanism for the auto-inhibition of hyperpolarization-activated cyclic nucleotide-gated (HCN) channel opening and its relief by cAMP.
Akimoto M, Zhang Z, Boulton S, Selvaratnam R, VanSchouwen B, Gloyd M, Accili EA, Lange OF, Melacini G
J Biol Chem 289 22205-20 (2014)
PMID: 24878962

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195214 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 14.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3Q4 (Residues: 579-707; Coverage: 11%)
Gene name: HCN4
Sequence domains: Cyclic nucleotide-binding domain
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 68%
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.
Wei et al. (2016)
7 more

6 mentions without citation

Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function.
Saponaro et al. (2014)
5 more