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Article

Conserved residues within the putative S4-S5 region serve distinct functions among thermosensitive vanilloid transient receptor potential (TRPV) channels.

The Journal of biological chemistry - 31 Dec 2010

Boukalova Stepana, Marsakova Lenka, Teisinger Jan, Vlachova Viktorie

Abstract excerpt

The vanilloid transient receptor potential channel TRPV1 is a tetrameric six-transmembrane segment (S1-S6) channel that can be synergistically activated by various proalgesic agents such as capsaicin, protons, heat, or highly depolarizing voltages, and also by 2-aminoethoxydiphenyl borate (2-APB)...

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Source

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Identifiers

PMID: 21044960
DOI: 10.1074/jbc.M110.145466
PMCID: PMC3009871

Genes

TRPV1
TRPV2
TRPV3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-21044960-2026-09-04.1. Manifest publication-graph-cohort-2026-09-04.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conserved residues within the putative S4-S5 region serve distinct functions among thermosensitive vanilloid transient receptor potential (TRPV) channels.PMID 21044960Read ↗

Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1).Semantic proximity Read ↗

TRPV1.Semantic proximity Read ↗

Identification of molecular determinants of channel gating in the transient receptor potential box of vanilloid receptor I.Semantic proximity Read ↗

Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain.Semantic proximity Read ↗

Structural modeling and patch-clamp analysis of pain-related mutation TRPA1-N855S reveal inter-subunit salt bridges stabilizing the channel open state.Semantic proximity Read ↗

Structural origins of species-specific differences in TRPV2 activation.Semantic proximity Read ↗

The S4---S5 linker - gearbox of TRP channel gating.Semantic proximity Read ↗

TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli.Semantic proximity Read ↗

The TRPV4 channel.Semantic proximity Read ↗

Protons stabilize the closed conformation of gain-of-function mutants of the TRPV1 channel.Semantic proximity Read ↗

A competing hydrophobic tug on L596 to the membrane core unlatches S4-S5 linker elbow from TRP helix and allows TRPV4 channel to open.Semantic proximity Read ↗

Ratio of hydrophobic-hydrophilic and positive-negative residues at lipid-water-interface influences surface expression and channel-gating of TRPV1Semantic proximity Read ↗

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