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Sequence and structural conservation reveal fingerprint residues in TRP channels
Transient receptor potential (TRP) proteins are a large family of cation-selective channels, surpassed in variety only by voltage-gated potassium channels. Detailed molecular mechanisms governing how membrane voltage, ligand binding, or temperature can induce conformational changes promoting the ope...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9242649/ https://www.ncbi.nlm.nih.gov/pubmed/35686986 http://dx.doi.org/10.7554/eLife.73645 |
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author | Cabezas-Bratesco, Deny Mcgee, Francisco A Colenso, Charlotte K Zavala, Kattina Granata, Daniele Carnevale, Vincenzo Opazo, Juan C Brauchi, Sebastian E |
author_facet | Cabezas-Bratesco, Deny Mcgee, Francisco A Colenso, Charlotte K Zavala, Kattina Granata, Daniele Carnevale, Vincenzo Opazo, Juan C Brauchi, Sebastian E |
author_sort | Cabezas-Bratesco, Deny |
collection | PubMed |
description | Transient receptor potential (TRP) proteins are a large family of cation-selective channels, surpassed in variety only by voltage-gated potassium channels. Detailed molecular mechanisms governing how membrane voltage, ligand binding, or temperature can induce conformational changes promoting the open state in TRP channels are still a matter of debate. Aiming to unveil distinctive structural features common to the transmembrane domains within the TRP family, we performed phylogenetic reconstruction, sequence statistics, and structural analysis over a large set of TRP channel genes. Here, we report an exceptionally conserved set of residues. This fingerprint is composed of twelve residues localized at equivalent three-dimensional positions in TRP channels from the different subtypes. Moreover, these amino acids are arranged in three groups, connected by a set of aromatics located at the core of the transmembrane structure. We hypothesize that differences in the connectivity between these different groups of residues harbor the apparent differences in coupling strategies used by TRP subgroups. |
format | Online Article Text |
id | pubmed-9242649 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-92426492022-06-30 Sequence and structural conservation reveal fingerprint residues in TRP channels Cabezas-Bratesco, Deny Mcgee, Francisco A Colenso, Charlotte K Zavala, Kattina Granata, Daniele Carnevale, Vincenzo Opazo, Juan C Brauchi, Sebastian E eLife Evolutionary Biology Transient receptor potential (TRP) proteins are a large family of cation-selective channels, surpassed in variety only by voltage-gated potassium channels. Detailed molecular mechanisms governing how membrane voltage, ligand binding, or temperature can induce conformational changes promoting the open state in TRP channels are still a matter of debate. Aiming to unveil distinctive structural features common to the transmembrane domains within the TRP family, we performed phylogenetic reconstruction, sequence statistics, and structural analysis over a large set of TRP channel genes. Here, we report an exceptionally conserved set of residues. This fingerprint is composed of twelve residues localized at equivalent three-dimensional positions in TRP channels from the different subtypes. Moreover, these amino acids are arranged in three groups, connected by a set of aromatics located at the core of the transmembrane structure. We hypothesize that differences in the connectivity between these different groups of residues harbor the apparent differences in coupling strategies used by TRP subgroups. eLife Sciences Publications, Ltd 2022-06-10 /pmc/articles/PMC9242649/ /pubmed/35686986 http://dx.doi.org/10.7554/eLife.73645 Text en © 2022, Cabezas-Bratesco, Mcgee et al https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Evolutionary Biology Cabezas-Bratesco, Deny Mcgee, Francisco A Colenso, Charlotte K Zavala, Kattina Granata, Daniele Carnevale, Vincenzo Opazo, Juan C Brauchi, Sebastian E Sequence and structural conservation reveal fingerprint residues in TRP channels |
title | Sequence and structural conservation reveal fingerprint residues in TRP channels |
title_full | Sequence and structural conservation reveal fingerprint residues in TRP channels |
title_fullStr | Sequence and structural conservation reveal fingerprint residues in TRP channels |
title_full_unstemmed | Sequence and structural conservation reveal fingerprint residues in TRP channels |
title_short | Sequence and structural conservation reveal fingerprint residues in TRP channels |
title_sort | sequence and structural conservation reveal fingerprint residues in trp channels |
topic | Evolutionary Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9242649/ https://www.ncbi.nlm.nih.gov/pubmed/35686986 http://dx.doi.org/10.7554/eLife.73645 |
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