5F1C

Crystal structure of an invertebrate P2X receptor from the Gulf Coast tick in the presence of ATP and Zn2+ ion at 2.9 Angstroms

5F1C の概要

• エントリーDOI: 10.2210/pdb5f1c/pdb
• 分子名称: Putative uncharacterized protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (5 entities in total)
• 機能のキーワード: ligand, complex, channel, agonist, membrane protein
• 由来する生物種: Amblyomma maculatum (Gulf Coast tick)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 124030.09

構造登録者

Kasuya, G.,Hattori, M.,Ishitani, R.,Nureki, O. (登録日: 2015-11-30, 公開日: 2016-03-16, 最終更新日: 2024-10-30)

主引用文献

Kasuya, G.,Fujiwara, Y.,Takemoto, M.,Dohmae, N.,Nakada-Nakura, Y.,Ishitani, R.,Hattori, M.,Nureki, O.
Structural Insights into Divalent Cation Modulations of ATP-Gated P2X Receptor Channels
Cell Rep, 14:932-944, 2016

PubMed Abstract: P2X receptors are trimeric ATP-gated cation channels involved in physiological processes ranging widely from neurotransmission to pain and taste signal transduction. The modulation of the channel gating, including that by divalent cations, contributes to these diverse physiological functions of P2X receptors. Here, we report the crystal structure of an invertebrate P2X receptor from the Gulf Coast tick Amblyomma maculatum in the presence of ATP and Zn(2+) ion, together with electrophysiological and computational analyses. The structure revealed two distinct metal binding sites, M1 and M2, in the extracellular region. The M1 site, located at the trimer interface, is responsible for Zn(2+) potentiation by facilitating the structural change of the extracellular domain for pore opening. In contrast, the M2 site, coupled with the ATP binding site, might contribute to regulation by Mg(2+). Overall, our work provides structural insights into the divalent cation modulations of P2X receptors.

PubMed: 26804916
DOI: 10.1016/j.celrep.2015.12.087

実験手法

X-RAY DIFFRACTION (2.9 Å)