Loading...
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.
Cabezas-Bratesco, Deny
Mcgee, Francisco A.
Colenso, Charlotte K.
Zavala, Kattina
Granata, Daniele
Carnevale, Vincenzo
Opazo, Juan C.
Brauchi, Sebastian E.
Citations
Altmetric:
Genre
Journal article
Date
2022-06-10
Advisor
Committee member
Department
Biology
Subject
Permanent link to this record
Collections
Research Projects
Organizational Units
Journal Issue
DOI
http://dx.doi.org/10.7554/elife.73645
Abstract
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.
Description
Citation
Deny Cabezas-Bratesco Francisco A Mcgee Charlotte K Colenso Kattina Zavala Daniele Granata Vincenzo Carnevale Juan C Opazo Sebastian E Brauchi (2022) Sequence and structural conservation reveal fingerprint residues in TRP channels eLife 11:e73645. https://doi.org/10.7554/eLife.73645
Citation to related work
eLife Sciences Publications
Has part
eLife, Vol. 11
ADA compliance
For Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu