TRP ion channels: Proteins with conformational flexibility
Autor: | León D. Islas, Tamara Rosenbaum, Luis B. Tovar-y-Romo, Francisco Torres-Quiroz, Ana E. López-Romero, Ileana Hernández-Araiza |
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Rok vydání: | 2019 |
Předmět: |
0301 basic medicine
Flexibility (anatomy) Protein Conformation Biophysics Review Biochemistry structure-function lipid-protein interactions 03 medical and health sciences Transient receptor potential channel Transient Receptor Potential Channels 0302 clinical medicine medicine Animals Humans TRP Channels Patch clamp Ion channel chemistry.chemical_classification Chemistry Resolution (electron density) Amino acid Electrophysiology 030104 developmental biology medicine.anatomical_structure Ion channels Multigene Family 030217 neurology & neurosurgery Function (biology) Signal Transduction |
Zdroj: | Channels |
ISSN: | 1933-6969 1933-6950 |
DOI: | 10.1080/19336950.2019.1626793 |
Popis: | Ion channels display conformational changes in response to binding of their agonists and antagonists. The study of the relationships between the structure and the function of these proteins has witnessed considerable advances in the last two decades using a combination of techniques, which include electrophysiology, optical approaches (i.e. patch clamp fluorometry, incorporation of non-canonic amino acids, etc.), molecular biology (mutations in different regions of ion channels to determine their role in function) and those that have permitted the resolution of their structures in detail (X-ray crystallography and cryo-electron microscopy). The possibility of making correlations among structural components and functional traits in ion channels has allowed for more refined conclusions on how these proteins work at the molecular level. With the cloning and description of the family of Transient Receptor Potential (TRP) channels, our understanding of several sensory-related processes has also greatly moved forward. The response of these proteins to several agonists, their regulation by signaling pathways as well as by protein-protein and lipid-protein interactions and, in some cases, their biophysical characteristics have been studied thoroughly and, recently, with the resolution of their structures, the field has experienced a new boom. This review article focuses on the conformational changes in the pores, concentrating on some members of the TRP family of ion channels (TRPV and TRPA subfamilies) that result in changes in their single-channel conductances, a phenomenon that may lead to fine-tuning the electrical response to a given agonist in a cell. |
Databáze: | OpenAIRE |
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