Discrimination between cyclic nucleotides in a cyclic nucleotide-gated ion channel.


Journal

Nature structural & molecular biology
ISSN: 1545-9985
Titre abrégé: Nat Struct Mol Biol
Pays: United States
ID NLM: 101186374

Informations de publication

Date de publication:
04 2023
Historique:
received: 24 07 2022
accepted: 24 02 2023
medline: 20 4 2023
pubmed: 28 3 2023
entrez: 27 3 2023
Statut: ppublish

Résumé

Cyclic nucleotide-gated ion channels are crucial in many physiological processes such as vision and pacemaking in the heart. SthK is a prokaryotic homolog with high sequence and structure similarities to hyperpolarization-activated and cyclic nucleotide-modulated and cyclic nucleotide-gated channels, especially at the level of the cyclic nucleotide binding domains (CNBDs). Functional measurements showed that cyclic adenosine monophosphate (cAMP) is a channel activator while cyclic guanosine monophosphate (cGMP) barely leads to pore opening. Here, using atomic force microscopy single-molecule force spectroscopy and force probe molecular dynamics simulations, we unravel quantitatively and at the atomic level how CNBDs discriminate between cyclic nucleotides. We find that cAMP binds to the SthK CNBD slightly stronger than cGMP and accesses a deep-bound state that a cGMP-bound CNBD cannot reach. We propose that the deep binding of cAMP is the discriminatory state that is essential for cAMP-dependent channel activation.

Identifiants

pubmed: 36973509
doi: 10.1038/s41594-023-00955-3
pii: 10.1038/s41594-023-00955-3
pmc: PMC10194703
mid: NIHMS1889032
doi:

Substances chimiques

Nucleotides, Cyclic 0
Cyclic Nucleotide-Gated Cation Channels 0
Cyclic AMP E0399OZS9N
Cyclic GMP H2D2X058MU

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

512-520

Subventions

Organisme : American Heart Association-American Stroke Association
ID : 18POST33960309
Pays : United States
Organisme : NCCIH NIH HHS
ID : DP1 AT010874
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM124451
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS110790
Pays : United States

Informations de copyright

© 2023. The Author(s), under exclusive licence to Springer Nature America, Inc.

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Auteurs

Yangang Pan (Y)

Department of Anesthesiology, Weill Cornell Medicine, New York, NY, USA.

Emmi Pohjolainen (E)

Max Planck Institute for Multidisciplinary Sciences, Theoretical and Computational Biophysics Department, Goettingen, Germany.

Philipp A M Schmidpeter (PAM)

Department of Anesthesiology, Weill Cornell Medicine, New York, NY, USA.

Andrea C Vaiana (AC)

Max Planck Institute for Multidisciplinary Sciences, Theoretical and Computational Biophysics Department, Goettingen, Germany.
Institute of Biophysics, National Research Council, Palermo, Italy.

Crina M Nimigean (CM)

Department of Anesthesiology, Weill Cornell Medicine, New York, NY, USA.
Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY, USA.

Helmut Grubmüller (H)

Max Planck Institute for Multidisciplinary Sciences, Theoretical and Computational Biophysics Department, Goettingen, Germany.

Simon Scheuring (S)

Department of Anesthesiology, Weill Cornell Medicine, New York, NY, USA. sis2019@med.cornell.edu.
Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY, USA. sis2019@med.cornell.edu.

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