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-Structure paper
タイトル | Structure of the full-length TRPV2 channel by cryo-EM. |
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ジャーナル・号・ページ | Nat Commun, Vol. 7, Page 11130, Year 2016 |
掲載日 | 2016年3月29日 |
著者 | Kevin W Huynh / Matthew R Cohen / Jiansen Jiang / Amrita Samanta / David T Lodowski / Z Hong Zhou / Vera Y Moiseenkova-Bell / |
PubMed 要旨 | Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a 'minimal' TRP vanilloid ...Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a 'minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2-6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at ∼5 Å resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels. |
リンク | Nat Commun / PubMed:27021073 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.4 - 4.7 Å |
構造データ | |
由来 |
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キーワード | TRANSPORT PROTEIN / TRPV2 ion channel |