Conformational ensemble of the human TRPV3 ion channel
| العنوان: | Conformational ensemble of the human TRPV3 ion channel |
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| المؤلفون: | William F. Borschel, Gabriel C. Lander, Marscha Hirschi, Lejla Zubcevic, Mark A. Herzik, Seok-Yong Lee, Mengyu Wu, Albert S. Song |
| المصدر: | Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018) Nature Communications |
| بيانات النشر: | Nature Portfolio, 2018. |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | Boron Compounds, Protein Conformation, alpha-Helical, 0301 basic medicine, Agonist, TRPV3, Hot Temperature, medicine.drug_class, Science, Biophysics, Regulator, TRPV Cation Channels, General Physics and Astronomy, Gating, 010402 general chemistry, 01 natural sciences, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Transient receptor potential channel, 0302 clinical medicine, Protein structure, medicine, Humans, lcsh:Science, Ion channel, Sensitization, 030304 developmental biology, Congenital skin disorder, 0303 health sciences, Multidisciplinary, Chemistry, Cryoelectron Microscopy, General Chemistry, Ligand (biochemistry), 0104 chemical sciences, 3. Good health, 030104 developmental biology, medicine.anatomical_structure, lcsh:Q, lipids (amino acids, peptides, and proteins), 030217 neurology & neurosurgery |
| الوصف: | Transient receptor potential vanilloid channel 3 (TRPV3), a member of the thermosensitive TRP (thermoTRPV) channels, is activated by warm temperatures and serves as a key regulator of normal skin physiology through the release of pro-inflammatory messengers. Mutations in trpv3 have been identified as the cause of the congenital skin disorder, Olmsted syndrome. Unlike other members of the thermoTRPV channel family, TRPV3 sensitizes upon repeated stimulation, yet a lack of structural information about the channel precludes a molecular-level understanding of TRPV3 sensitization and gating. Here, we present the cryo-electron microscopy structures of apo and sensitized human TRPV3, as well as several structures of TRPV3 in the presence of the common thermoTRPV agonist 2-aminoethoxydiphenyl borate (2-APB). Our results show α-to-π-helix transitions in the S6 during sensitization, and suggest a critical role for the S4-S5 linker π-helix during ligand-dependent gating. Transient receptor potential vanilloid channel 3 (TRPV3) responds to temperature and sensitizes upon repeated stimulation with either heat or agonists. Here authors present the cryo-EM structures of apo and sensitized human TRPV3 and describe the structural basis of sensitization. |
| اللغة: | English |
| تدمد: | 2041-1723 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::267025fafc80edd88354362f398046aa https://doaj.org/article/2ea7563e099f422d909405e9c45dad14 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....267025fafc80edd88354362f398046aa |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20411723 |
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