7YVB

Aplysia californica FaNaC in ligand bound state

7YVB の概要

• エントリーDOI: 10.2210/pdb7yvb/pdb
• EMDBエントリー: 34122
• 分子名称: FMRFamide-gated Na+ channel, Phe-Met-Arg-Phe-amide, PHENYLALANINE AMIDE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: neuropeptide, ion channel, fmrfamide, transport protein
• 由来する生物種: Aplysia californica (California sea hare); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 238131.28

構造登録者

Chen, Q.F.,Liu, F.L.,Dang, Y.,Feng, H.,Zhang, Z.,Ye, S. (登録日: 2022-08-19, 公開日: 2023-08-09, 最終更新日: 2025-06-25)

主引用文献

Liu, F.,Dang, Y.,Li, L.,Feng, H.,Li, J.,Wang, H.,Zhang, X.,Zhang, Z.,Ye, S.,Tian, Y.,Chen, Q.
Structure and mechanism of a neuropeptide-activated channel in the ENaC/DEG superfamily.
Nat.Chem.Biol., 19:1276-1285, 2023

PubMed Abstract: Phe-Met-Arg-Phe-amide (FMRFamide)-activated sodium channels (FaNaCs) are a family of channels activated by the neuropeptide FMRFamide, and, to date, the underlying ligand gating mechanism remains unknown. Here we present the high-resolution cryo-electron microscopy structures of Aplysia californica FaNaC in both apo and FMRFamide-bound states. AcFaNaC forms a chalice-shaped trimer and possesses several notable features, including two FaNaC-specific insertion regions, a distinct finger domain and non-domain-swapped transmembrane helix 2 in the transmembrane domain (TMD). One FMRFamide binds to each subunit in a cleft located in the top-most region of the extracellular domain, with participation of residues from the neighboring subunit. Bound FMRFamide adopts an extended conformation. FMRFamide binds tightly to A. californica FaNaC in an N terminus-in manner, which causes collapse of the binding cleft and induces large local conformational rearrangements. Such conformational changes are propagated downward toward the TMD via the palm domain, possibly resulting in outward movement of the TMD and dilation of the ion conduction pore.

PubMed: 37550431
DOI: 10.1038/s41589-023-01401-7

実験手法

ELECTRON MICROSCOPY (2.9 Å)