3MRA

M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES

3MRA の概要

• エントリーDOI: 10.2210/pdb3mra/pdb
• 分子名称: Acetylcholine receptor subunit alpha (1 entity in total)
• 機能のキーワード: transmembrane segment m3 of nachr, receptor, ion-channel, membrane protein, transmembrane segment, alpha-helix
• 由来する生物種: Tetronarce californica (Pacific electric ray)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2951.61

構造登録者

Lugovskoy, A.A.,Maslennikov, I.V.,Utkin, Y.N.,Tsetlin, V.I.,Cohen, J.B.,Arseniev, A.S. (登録日: 1997-07-15, 公開日: 1998-01-21, 最終更新日: 2024-05-01)

主引用文献

Lugovskoy, A.A.,Maslennikov, I.V.,Utkin, Y.N.,Tsetlin, V.I.,Cohen, J.B.,Arseniev, A.S.
Spatial structure of the M3 transmembrane segment of the nicotinic acetylcholine receptor alpha subunit.
Eur.J.Biochem., 255:455-461, 1998

PubMed Abstract: The three-dimensional structure of a synthetic peptide corresponding to the putative transmembrane segment M3 (amino acid residues 277-301) of the alpha subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by means of two-dimensional 1H-NMR spectroscopy in a chloroform/methanol (1:1) mixture containing 0.1 M LiClO4. Complete resonance assignment has been performed using double-quantum-filtered COSY (DQF-COSY), TOCSY and NOESY spectra. The spatial structure has been calculated using the Diana program on the basis of integrated intensities of NOESY spectra. HN-C(alpha)H and HC(alpha)-C(beta)H spin-spin coupling constants. Residues 279-297 of M3 form a right-handed helix (root mean square deviation is 0.032 nm for backbone atoms and 0.088 nm for all heavy atoms). The conformations of the 17 side chains have been unambiguously determined. The obtained structure is in accord with the photolabeling pattern of the membrane nicotinic acetylcholine receptor (nAChR) which suggests alpha-helical structure of M3 in the labeled portion [Blanton, M. P. & Cohen, J. B. (1994) Biochemistry 33, 2859-2872].

PubMed: 9716388
DOI: 10.1046/j.1432-1327.1998.2550455.x

実験手法

SOLUTION NMR