› 2mpf

Solution NMR

Solution structure human HCN2 CNBD in the cAMP-unbound state

Released:
DOI: 10.2210/pdb2mpf/pdb
PDB entry 2mpf coloured by chain, ensemble of 20 models, front view.
PDB entry 2mpf coloured by chain, ensemble of 20 models, side view.
PDB entry 2mpf coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function.
Saponaro A, Pauleta SR, Cantini F, Matzapetakis M, Hammann C, Donadoni C, Hu L, Thiel G, Banci L, Santoro B, Moroni A
Proc Natl Acad Sci U S A 111 14577-82 (2014)
PMID: 25197093

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-193910 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UL51 (Residues: 521-672; Coverage: 17%)
Gene names: BCNG2, HCN2
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: 87%
Refinement method: torsion angle dynamics, molecular dynamics
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

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

4 mentions without citation

cyclic AMP Regulation and Its Command in the Pacemaker Channel HCN4.
Porro et al. (2020)
3 more