Voltage vs. Ligand II: Structural insights of the intrinsic flexibility in cyclic nucleotide-gated channels.
CNG channels
Local flexibility
pore domain; ; TolQ
voltage sensor
Journal
Channels (Austin, Tex.)
ISSN: 1933-6969
Titre abrégé: Channels (Austin)
Pays: United States
ID NLM: 101321614
Informations de publication
Date de publication:
12 2019
12 2019
Historique:
entrez:
26
9
2019
pubmed:
26
9
2019
medline:
14
7
2020
Statut:
ppublish
Résumé
In the preceding article, we present a flexibility analysis of the voltage-gated ion channel (VGIC) superfamily. In this study, we describe in detail the flexibility profile of the voltage-sensor domain (VSD) and the pore domain (PD) concerning the evolution of 6TM ion channels. In particular, we highlight the role of flexibility in the emergence of CNG channels and describe a significant level of sequence similarity between the archetypical VSD and the TolQ proteins. A highly flexible S4-like segment exhibiting Lys instead Arg for these membrane proteins is reported. Sequence analysis indicates that, in addition to this S4-like segment, TolQ proteins also show similarity with specific motifs in S2 and S3 from typical V-sensors. Notably, S3 flexibility profiles from typical VSDs and S3-like in TolQ proteins are also similar. Interestingly, TolQ from early divergent prokaryotes are comparatively more flexible than those in modern counterparts or true V-sensors. Regarding the PD, we also found that 2TM K
Identifiants
pubmed: 31552786
doi: 10.1080/19336950.2019.1666456
pmc: PMC6768053
doi:
Substances chimiques
Bacterial Proteins
0
Cyclic Nucleotide-Gated Cation Channels
0
Ligands
0
Nucleotides, Cyclic
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
382-399Références
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