Sequence and structural conservation reveal fingerprint residues in TRP channels
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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Jun 10, 2022
- Source ID
- 10.7554/elife.73645
Entities
People
- Charlotte K Colenso
- Daniele Granata
- Deny Cabezas-bratesco
- Francisco A Mcgee
- Juan C. Opazo
- Kattina Zavala
- Sebastian Brauchi
- Vincenzo Carnevale
Organizations
- Austral University of Chile
- Chilean National Agency for Research and Development
- Howard Hughes Medical Institute
- Millennium Nucleus of Ion Channel Associated Diseases
- National Fund for Scientific and Technological Development
- National Institutes of Health
- National Science Foundation
- Temple University
- United States Army
- University of Bristol