3mra
From Proteopedia
(New page: 200px<br /><applet load="3mra" size="450" color="white" frame="true" align="right" spinBox="true" caption="3mra" /> '''M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF...) |
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| - | [[Image:3mra.jpg|left|200px]]<br /><applet load="3mra" size=" | + | [[Image:3mra.jpg|left|200px]]<br /><applet load="3mra" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3mra" /> | caption="3mra" /> | ||
'''M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES'''<br /> | '''M3 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 15 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of a synthetic peptide corresponding to | + | 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== | ==About this Structure== | ||
| - | 3MRA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http:// | + | 3MRA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MRA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
| - | [[Category: Arseniev, A | + | [[Category: Arseniev, A S.]] |
| - | [[Category: Cohen, J | + | [[Category: Cohen, J B.]] |
| - | [[Category: Lugovskoy, A | + | [[Category: Lugovskoy, A A.]] |
| - | [[Category: Maslennikov, I | + | [[Category: Maslennikov, I V.]] |
| - | [[Category: Tsetlin, V | + | [[Category: Tsetlin, V I.]] |
| - | [[Category: Utkin, Y | + | [[Category: Utkin, Y N.]] |
[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
[[Category: ion-channel]] | [[Category: ion-channel]] | ||
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[[Category: transmembrane segment m3 of nachr]] | [[Category: transmembrane segment m3 of nachr]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:27 2008'' |
Revision as of 17:10, 21 February 2008
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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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