3mra
From Proteopedia
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M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES
Overview
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].
About this Structure
3MRA is a Single protein structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.
Reference
Spatial structure of the M3 transmembrane segment of the nicotinic acetylcholine receptor alpha subunit., Lugovskoy AA, Maslennikov IV, Utkin YN, Tsetlin VI, Cohen JB, Arseniev AS, Eur J Biochem. 1998 Jul 15;255(2):455-61. PMID:9716388
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