A structural view of ligand-dependent activation in thermoTRP channels
Transient Receptor Potential (TRP) proteins are a large family of ion channels, grouped into<br/>seven sub-families. Although great advances have been made regarding the activation and<br/>modulation of TRP channel activity, detailed molecular mechanisms governing TRP<br/>channel g...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2014-05-01
|
| Series: | Frontiers in Physiology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fphys.2014.00171/full |
| _version_ | 1818198126692925440 |
|---|---|
| author | Ximena eSteinberg Ximena eSteinberg Carolyne eLespay-Rebolledo Sebastian eBrauchi |
| author_facet | Ximena eSteinberg Ximena eSteinberg Carolyne eLespay-Rebolledo Sebastian eBrauchi |
| author_sort | Ximena eSteinberg |
| collection | DOAJ |
| description | Transient Receptor Potential (TRP) proteins are a large family of ion channels, grouped into<br/>seven sub-families. Although great advances have been made regarding the activation and<br/>modulation of TRP channel activity, detailed molecular mechanisms governing TRP<br/>channel gating are still needed. Sensitive to electric, chemical, mechanical, and thermal<br/>cues, TRP channels are tightly associated with the detection and integration of sensory<br/>input, emerging as a model to study the polymodal activation of ion channel proteins.<br/>Among TRP channels, the temperature-activated kind constitute a subgroup by itself,<br/>formed by Vanilloid receptors 1-4, Melastatin receptors 2, 4, 5 and 8, TRPC5, and TRPA1.<br/>Some of the so-called thermoTRP channels participate in the detection of noxious stimuli<br/>making them an interesting pharmacological target for the treatment of pain. However, the<br/>poor specificity of the compounds available in the market represents an important obstacle<br/>to overcome. Understanding the molecular mechanics underlying ligand-dependent<br/>modulation of TRP channels may help with the rational design of novel synthetic<br/>analgesics. The present review focuses on the structural basis of ligand-dependent<br/>activation of TRPV1 and TRPM8 channels. Special attention is drawn to the dissection of<br/>ligand-binding sites within TRPV1, PIP 2 -dependent modulation of TRP channels, and the<br/>structure of natural and synthetic ligands. |
| first_indexed | 2024-12-12T02:00:55Z |
| format | Article |
| id | doaj.art-48c5fb9cec114b12834c7a4338582726 |
| institution | Directory Open Access Journal |
| issn | 1664-042X |
| language | English |
| last_indexed | 2024-12-12T02:00:55Z |
| publishDate | 2014-05-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Physiology |
| spelling | doaj.art-48c5fb9cec114b12834c7a43385827262022-12-22T00:42:11ZengFrontiers Media S.A.Frontiers in Physiology1664-042X2014-05-01510.3389/fphys.2014.0017182295A structural view of ligand-dependent activation in thermoTRP channelsXimena eSteinberg0Ximena eSteinberg1Carolyne eLespay-Rebolledo2Sebastian eBrauchi3Universidad Austral de ChileUniversidad Austral de ChileUniversidad de ChileUniversidad Austral de ChileTransient Receptor Potential (TRP) proteins are a large family of ion channels, grouped into<br/>seven sub-families. Although great advances have been made regarding the activation and<br/>modulation of TRP channel activity, detailed molecular mechanisms governing TRP<br/>channel gating are still needed. Sensitive to electric, chemical, mechanical, and thermal<br/>cues, TRP channels are tightly associated with the detection and integration of sensory<br/>input, emerging as a model to study the polymodal activation of ion channel proteins.<br/>Among TRP channels, the temperature-activated kind constitute a subgroup by itself,<br/>formed by Vanilloid receptors 1-4, Melastatin receptors 2, 4, 5 and 8, TRPC5, and TRPA1.<br/>Some of the so-called thermoTRP channels participate in the detection of noxious stimuli<br/>making them an interesting pharmacological target for the treatment of pain. However, the<br/>poor specificity of the compounds available in the market represents an important obstacle<br/>to overcome. Understanding the molecular mechanics underlying ligand-dependent<br/>modulation of TRP channels may help with the rational design of novel synthetic<br/>analgesics. The present review focuses on the structural basis of ligand-dependent<br/>activation of TRPV1 and TRPM8 channels. Special attention is drawn to the dissection of<br/>ligand-binding sites within TRPV1, PIP 2 -dependent modulation of TRP channels, and the<br/>structure of natural and synthetic ligands.http://journal.frontiersin.org/Journal/10.3389/fphys.2014.00171/fullCapsaicinMentholStructureTRPV1TRP channelsPIP2 |
| spellingShingle | Ximena eSteinberg Ximena eSteinberg Carolyne eLespay-Rebolledo Sebastian eBrauchi A structural view of ligand-dependent activation in thermoTRP channels Frontiers in Physiology Capsaicin Menthol Structure TRPV1 TRP channels PIP2 |
| title | A structural view of ligand-dependent activation in thermoTRP channels |
| title_full | A structural view of ligand-dependent activation in thermoTRP channels |
| title_fullStr | A structural view of ligand-dependent activation in thermoTRP channels |
| title_full_unstemmed | A structural view of ligand-dependent activation in thermoTRP channels |
| title_short | A structural view of ligand-dependent activation in thermoTRP channels |
| title_sort | structural view of ligand dependent activation in thermotrp channels |
| topic | Capsaicin Menthol Structure TRPV1 TRP channels PIP2 |
| url | http://journal.frontiersin.org/Journal/10.3389/fphys.2014.00171/full |
| work_keys_str_mv | AT ximenaesteinberg astructuralviewofliganddependentactivationinthermotrpchannels AT ximenaesteinberg astructuralviewofliganddependentactivationinthermotrpchannels AT carolyneelespayrebolledo astructuralviewofliganddependentactivationinthermotrpchannels AT sebastianebrauchi astructuralviewofliganddependentactivationinthermotrpchannels AT ximenaesteinberg structuralviewofliganddependentactivationinthermotrpchannels AT ximenaesteinberg structuralviewofliganddependentactivationinthermotrpchannels AT carolyneelespayrebolledo structuralviewofliganddependentactivationinthermotrpchannels AT sebastianebrauchi structuralviewofliganddependentactivationinthermotrpchannels |