Thermodynamic profile of mutual subunit control in a heteromeric receptor.
Gibbs free energy
concatenated cyclic nucleotide-gated channels
coupled allosteric models
heteromeric membrane receptors
microscopic cooperativity
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
27 07 2021
27 07 2021
Historique:
entrez:
24
7
2021
pubmed:
25
7
2021
medline:
15
12
2021
Statut:
ppublish
Résumé
Cyclic nucleotide-gated (CNG) ion channels of olfactory neurons are tetrameric membrane receptors that are composed of two A2 subunits, one A4 subunit, and one B1b subunit. Each subunit carries a cyclic nucleotide-binding domain in the carboxyl terminus, and the channels are activated by the binding of cyclic nucleotides. The mechanism of cooperative channel activation is still elusive. Using a complete set of engineered concatenated olfactory CNG channels, with all combinations of disabled binding sites and fit analyses with systems of allosteric models, the thermodynamics of microscopic cooperativity for ligand binding was subunit- and state-specifically quantified. We show, for the closed channel, that preoccupation of each of the single subunits increases the affinity of each other subunit with a Gibbs free energy (
Identifiants
pubmed: 34301910
pii: 2100469118
doi: 10.1073/pnas.2100469118
pmc: PMC8325370
pii:
doi:
Substances chimiques
Cyclic Nucleotide-Gated Cation Channels
0
Ligands
0
Protein Subunits
0
Cyclic AMP
E0399OZS9N
Cyclic GMP
H2D2X058MU
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2021 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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