7WL2

Mouse Pendrin in bicarbonate and iodide buffer in inward state

7WL2 の概要

• エントリーDOI: 10.2210/pdb7wl2/pdb
• EMDBエントリー: 32574
• 分子名称: Pendrin (1 entity in total)
• 機能のキーワード: exchange, transport, slc, transport protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 171539.16

構造登録者

Liu, Q.Y.,Zhang, X.,Sun, L.,Chen, Z.G. (登録日: 2022-01-12, 公開日: 2023-04-12, 最終更新日: 2025-09-03)

主引用文献

Liu, Q.,Zhang, X.,Huang, H.,Chen, Y.,Wang, F.,Hao, A.,Zhan, W.,Mao, Q.,Hu, Y.,Han, L.,Sun, Y.,Zhang, M.,Liu, Z.,Li, G.L.,Zhang, W.,Shu, Y.,Sun, L.,Chen, Z.
Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger.
Nat Commun, 14:3012-3012, 2023

PubMed Abstract: Pendrin (SLC26A4) is an anion exchanger expressed in the apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder associated with sensorineural hearing loss, hypothyroid goiter, and reduced blood pressure. However its molecular structure has remained unknown, limiting our understanding of the structural basis of transport. Here, we determine the cryo-electron microscopy structures of mouse pendrin with symmetric and asymmetric homodimer conformations. The asymmetric homodimer consists of one inward-facing protomer and the other outward-facing protomer, representing coincident uptake and secretion- a unique state of pendrin as an electroneutral exchanger. The multiple conformations presented here provide an inverted alternate-access mechanism for anion exchange. The structural and functional data presented here disclose the properties of an anion exchange cleft and help understand the importance of disease-associated variants, which will shed light on the pendrin exchange mechanism.

PubMed: 37230976
DOI: 10.1038/s41467-023-38303-0

実験手法

ELECTRON MICROSCOPY (3.25 Å)