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TitleCyclic dinucleotides bind the C-linker of HCN4 to control channel cAMP responsiveness.
Journal, issue, pagesNat. Chem. Biol., Vol. 10, Page 457-462, Year 2014
Publish dateMay 7, 2013 (structure data deposition date)
AuthorsLolicato, M. / Bucchi, A. / Arrigoni, C. / Zucca, S. / Nardini, M. / Schroeder, I. / Simmons, K. / Aquila, M. / DiFrancesco, D. / Bolognesi, M. ...Lolicato, M. / Bucchi, A. / Arrigoni, C. / Zucca, S. / Nardini, M. / Schroeder, I. / Simmons, K. / Aquila, M. / DiFrancesco, D. / Bolognesi, M. / Schwede, F. / Kashin, D. / Fishwick, C.W. / Johnson, A.P. / Thiel, G. / Moroni, A.
External linksNat. Chem. Biol. / PubMed:24776929
MethodsX-ray diffraction
Resolution2.7 Å
Structure data

PDB-4kl1:
HCN4 CNBD in complex with cGMP
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-PCG:
CYCLIC GUANOSINE MONOPHOSPHATE

ChemComp-ACT:
ACETATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / CNBD / cAMP / cGMP / c-di-GMP / c-di-AMP / ion channel / HCN / Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel / cAMP binding / cGMP binding

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