A structural view of ligand-dependent activation in thermoTRP channels
Author
dc.contributor.author
Steinberg, Ximena
Author
dc.contributor.author
Lespay-Rebolledo, Carolyne
Author
dc.contributor.author
Brauchi, Sebastian
Admission date
dc.date.accessioned
2019-03-15T16:06:50Z
Available date
dc.date.available
2019-03-15T16:06:50Z
Publication date
dc.date.issued
2014
Cita de ítem
dc.identifier.citation
Frontiers in Physiology, Volumen 5 MAY,
Identifier
dc.identifier.issn
1664042X
Identifier
dc.identifier.other
10.3389/fphys.2014.00171
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/166215
Abstract
dc.description.abstract
Transient Receptor Potential (TRP) proteins are a large family of ion channels, grouped into seven sub-families. Although great advances have been made regarding the activation and modulation of TRP channel activity, detailed molecular mechanisms governing TRP channel gating are still needed. Sensitive to electric, chemical, mechanical, and thermal cues, TRP channels are tightly associated with the detection and integration of sensory input, emerging as a model to study the polymodal activation of ion channel proteins. Among TRP channels, the temperature-activated kind constitute a subgroup by itself, formed by Vanilloid receptors 1-4, Melastatin receptors 2, 4, 5, and 8, TRPC5, and TRPA1. Some of the so-called "thermoTRP" channels participate in the detection of noxious stimuli making them an interesting pharmacological target for the treatment of pain. However, the poor specificity of the compounds available in the market represents an important obstacle to overcome. Understanding th