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TitleGating movements and ion permeation in HCN4 pacemaker channels.
Journal, issue, pagesMol Cell, Vol. 81, Issue 14, Page 2929-22943.e6, Year 2021
Publish dateJul 15, 2021
AuthorsAndrea Saponaro / Daniel Bauer / M Hunter Giese / Paolo Swuec / Alessandro Porro / Federica Gasparri / Atiyeh Sadat Sharifzadeh / Antonio Chaves-Sanjuan / Laura Alberio / Giacomo Parisi / Gabriele Cerutti / Oliver B Clarke / Kay Hamacher / Henry M Colecraft / Filippo Mancia / Wayne A Hendrickson / Steven A Siegelbaum / Dario DiFrancesco / Martino Bolognesi / Gerhard Thiel / Bina Santoro / Anna Moroni /
PubMed AbstractThe HCN1-4 channel family is responsible for the hyperpolarization-activated cation current I/I that controls automaticity in cardiac and neuronal pacemaker cells. We present cryoelectron microscopy ...The HCN1-4 channel family is responsible for the hyperpolarization-activated cation current I/I that controls automaticity in cardiac and neuronal pacemaker cells. We present cryoelectron microscopy (cryo-EM) structures of HCN4 in the presence or absence of bound cAMP, displaying the pore domain in closed and open conformations. Analysis of cAMP-bound and -unbound structures sheds light on how ligand-induced transitions in the channel cytosolic portion mediate the effect of cAMP on channel gating and highlights the regulatory role of a Mg coordination site formed between the C-linker and the S4-S5 linker. Comparison of open/closed pore states shows that the cytosolic gate opens through concerted movements of the S5 and S6 transmembrane helices. Furthermore, in combination with molecular dynamics analyses, the open pore structures provide insights into the mechanisms of K/Na permeation. Our results contribute mechanistic understanding on HCN channel gating, cyclic nucleotide-dependent modulation, and ion permeation.
External linksMol Cell / PubMed:34166608 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.6 Å
Structure data

12466

7nmn

EMDB-12466, PDB-7nmn:
Rabbit HCN4 stabilised in amphipol A8-35
Method: EM (single particle) / Resolution: 3.6 Å

12512

7np3

EMDB-12512, PDB-7np3:
cAMP-free rabbit HCN4 stabilized in LMNG-CHS detergent mixture
Method: EM (single particle) / Resolution: 3.3 Å

12513

7np4

EMDB-12513, PDB-7np4:
cAMP-bound rabbit HCN4 stabilized in LMNG-CHS detergent mixture
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-CMP:
ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE / Cyclic adenosine monophosphate

Source
  • oryctolagus cuniculus (rabbit)
KeywordsMEMBRANE PROTEIN / cryo-EM / ion channels / HCN channels / cAMP / ion transport

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