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-Structure paper
タイトル | Conformational ensemble of the human TRPV3 ion channel. |
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ジャーナル・号・ページ | Nat Commun, Vol. 9, Issue 1, Page 4773, Year 2018 |
掲載日 | 2018年11月14日 |
著者 | Lejla Zubcevic / Mark A Herzik / Mengyu Wu / William F Borschel / Marscha Hirschi / Albert S Song / Gabriel C Lander / Seok-Yong Lee / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:30429472 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.2 - 4.0 Å |
構造データ | EMDB-9115, PDB-6mho: EMDB-9117, PDB-6mhs: EMDB-9119, PDB-6mhv: |
由来 |
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キーワード | TRANSPORT PROTEIN / membrane protein / ion channel / TRP channel / calcium transport |