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TitleStructural basis for hyperpolarization-dependent opening of human HCN1 channel.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 5216, Year 2024
Publish dateJun 18, 2024
AuthorsVerena Burtscher / Jonathan Mount / Jian Huang / John Cowgill / Yongchang Chang / Kathleen Bickel / Jianhan Chen / Peng Yuan / Baron Chanda /
PubMed AbstractHyperpolarization and cyclic nucleotide (HCN) activated ion channels are critical for the automaticity of action potentials in pacemaking and rhythmic electrical circuits in the human body. Unlike ...Hyperpolarization and cyclic nucleotide (HCN) activated ion channels are critical for the automaticity of action potentials in pacemaking and rhythmic electrical circuits in the human body. Unlike most voltage-gated ion channels, the HCN and related plant ion channels activate upon membrane hyperpolarization. Although functional studies have identified residues in the interface between the voltage-sensing and pore domain as crucial for inverted electromechanical coupling, the structural mechanisms for this unusual voltage-dependence remain unclear. Here, we present cryo-electron microscopy structures of human HCN1 corresponding to Closed, Open, and a putative Intermediate state. Our structures reveal that the downward motion of the gating charges past the charge transfer center is accompanied by concomitant unwinding of the inner end of the S4 and S5 helices, disrupting the tight gating interface observed in the Closed state structure. This helix-coil transition at the intracellular gating interface accompanies a concerted iris-like dilation of the pore helices and underlies the reversed voltage dependence of HCN channels.
External linksNat Commun / PubMed:38890331 / PubMed Central
MethodsEM (single particle)
Resolution3.16 - 3.6 Å
Structure data

41036

8t4m

EMDB-41036, PDB-8t4m:
Closed human HCN1 F186C S264C bound to cAMP, reconstituted in LMNG + SPL
Method: EM (single particle) / Resolution: 3.16 Å

41040

8t4y

EMDB-41040, PDB-8t4y:
Human HCN1 F186C S264C C309A bound to cAMP, reconstituted in LMNG + SPL
Method: EM (single particle) / Resolution: 3.58 Å

41041

8t50

EMDB-41041, PDB-8t50:
Open human HCN1 F186C S264C bound to cAMP, reconstituted in LMNG + SPL
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-CMP:
ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Ion Channel / Membrane Protein

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