2M6B

Structure of full-length transmembrane domains of human glycine receptor alpha1 monomer subunit

2M6B の概要

• エントリーDOI: 10.2210/pdb2m6b/pdb
• 関連するPDBエントリー: 2M6I
• NMR情報: BMRB: 19126
• 分子名称: Full-Length Transmembrane Domains of Human Glycine Receptor alpha1 Subunit (1 entity in total)
• 機能のキーワード: glycine receptor, anion channel, transmembrane domain, membrane protein
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17320.32

構造登録者

Mowrey, D.,Cui, T.,Jia, Y.,Ma, D.,Makhov, A.M.,Zhang, P.,Tang, P.,Xu, Y. (登録日: 2013-03-28, 公開日: 2013-09-04, 最終更新日: 2024-05-15)

主引用文献

Mowrey, D.D.,Cui, T.,Jia, Y.,Ma, D.,Makhov, A.M.,Zhang, P.,Tang, P.,Xu, Y.
Open-Channel Structures of the Human Glycine Receptor alpha 1 Full-Length Transmembrane Domain.
Structure, 21:1897-1904, 2013

PubMed Abstract: Glycine receptors play a major role in mediating fast inhibitory neurotransmission in the spinal cord and brain stem, yet their high-resolution structures remain unsolved. We determined open-channel structures of the full-length transmembrane domain (TMD) of the human glycine receptor α1-subunit (hGlyR-α1) using nuclear magnetic resonance (NMR) spectroscopy and electron micrographs. hGlyR-α1 TMD spontaneously forms pentameric Cl(-)-conducting channels, with structures sharing overall topology observed in crystal structures of homologous bacterial and nematode pentameric ligand-gated ion channels (pLGICs). However, the mammalian hGlyR-α1 structures present several distinctive features, including a shorter, pore-lining TM2 helix with helical unwinding near the C-terminal end, a TM3 helical kink at A288 that partially overlaps with the homologous ivermectin-binding site in GluCl, and a highly dynamic segment between S267(15') of TM2 and A288 that likely affects allosteric modulations of channel function. Our structures provide additional templates for identifying potential drug targets in GlyRs and other mammalian pLGICs.

PubMed: 23994010
DOI: 10.1016/j.str.2013.07.014

実験手法

SOLUTION NMR