Cryo-electron microscopy structure of the TRPV2 ion channel
| Autor: | Mark A. Herzik, Seok-Yong Lee, Gabriel C. Lander, Ben C. Chung, Zhi-Rui Liu, Lejla Zubcevic |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation TRPV2 TRPV Cation Channels TRPV Article 03 medical and health sciences Transient receptor potential channel 0302 clinical medicine Protein structure Structural Biology Animals Molecular Biology Protein secondary structure Ion channel Chemistry Cryoelectron Microscopy Ankyrin Repeat 3. Good health Transmembrane domain Stretch-activated ion channel Crystallography 030104 developmental biology Biophysics Rabbits 030217 neurology & neurosurgery |
| Zdroj: | Nature structural & molecular biology |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsmb.3159 |
| Popis: | Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ~4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6. |
| Databáze: | OpenAIRE |
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