2K58

NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit

2K58 の概要

• エントリーDOI: 10.2210/pdb2k58/pdb
• 関連するPDBエントリー: 2K59
• 分子名称: Neuronal acetylcholine receptor subunit beta-2 (1 entity in total)
• 機能のキーワード: neuronal acetylcholine receptor, first transmembrane domain, beta 2 subunit, cell junction, disease mutation, epilepsy, glycoprotein, ion transport, ionic channel, membrane, polymorphism, postsynaptic cell membrane, synapse, transmembrane, transport, transport protein
• 細胞内の位置: Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P17787
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4014.88

構造登録者

Bondarenko, V.,Tang, P.,Xu, Y. (登録日: 2008-06-25, 公開日: 2008-07-08, 最終更新日: 2024-05-29)

主引用文献

Bondarenko, V.,Xu, Y.,Tang, P.
Structure of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit
Biophys.J., 92:1616-1622, 2007

PubMed Abstract: The recent cryoelectron microscopy structure of the Torpedo nicotinic acetylcholine receptor (nAChR) at 4-A resolution shows long helices for all transmembrane (TM) domains. This is in disagreement with several previous reports that the first TM domain of nAChR and other Cys-loop receptors are not entirely helical. In this study, we determined the structure and backbone dynamics of an extended segment encompassing the first TM domain (TM1e) of nAChR beta(2) subunit in dodecylphosphocholine micelles, using solution-state NMR and circular dichroism (CD) spectroscopy. Both CD and NMR results show less helicity in TM1e than in Torpedo nAChR structure (Protein Data Bank: 2BG9). The helical ending residues at the C-terminus are the same in the TM1e NMR structure and the Torpedo nAChR structure, but the helical starting residue (I-217) in TM1e is seven residues closer to the C-terminus. Interestingly, the helical starting residue is two residues before the highly conserved P-219, in accordance with the hypothesis that proline causes helical distortions at three residues preceding it. The NMR relaxation measurements show a dynamics pattern consistent with TM1e structure. The substantial nonhelical content adds greater flexibilities to TM1e, thereby implicating a different molecular basis for nAChR function compared to a longer and more rigid helical TM1.

PubMed: 17142275
DOI: 10.1529/biophysj.106.095364

実験手法

SOLUTION NMR