Lipid-dependent sequential allosteric activation of heat-sensing TRPV1 channels by anchor-stereoselective "hot" vanilloid compounds and analogs.
Active site stereoselectivity
Dominant steady-state ligand binding
Hydrogen bonding network
Ion channel
Lipid-ligand interaction
Recessive transient ligand binding
Sequential cooperativity
Journal
Biochemistry and biophysics reports
ISSN: 2405-5808
Titre abrégé: Biochem Biophys Rep
Pays: Netherlands
ID NLM: 101660999
Informations de publication
Date de publication:
Dec 2021
Dec 2021
Historique:
received:
31
05
2021
revised:
09
08
2021
accepted:
16
08
2021
entrez:
10
9
2021
pubmed:
11
9
2021
medline:
11
9
2021
Statut:
epublish
Résumé
Both a silent resident phosphatidylinositol lipid and a "hot" vanilloid agonist capsaicin or resiniferatoxin have been shown to share the same inter-subunit binding pocket between a voltage sensor like domain and a pore domain in TRPV1. However, how the vanilloid competes off the resident lipid for allosteric TRPV1 activation is unknown. Here, the
Identifiants
pubmed: 34504955
doi: 10.1016/j.bbrep.2021.101109
pii: S2405-5808(21)00204-1
pmc: PMC8416642
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
101109Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK045880
Pays : United States
Organisme : NIDDK NIH HHS
ID : R56 DK045880
Pays : United States
Organisme : NIDDK NIH HHS
ID : R56 DK056796
Pays : United States
Informations de copyright
© 2021 The Author.
Déclaration de conflit d'intérêts
The author declares no conflict of interest.
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