1dxz

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(New page: 200px<br /><applet load="1dxz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dxz" /> '''M2 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF...)
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[[Image:1dxz.gif|left|200px]]<br /><applet load="1dxz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dxz.gif|left|200px]]<br /><applet load="1dxz" size="350" color="white" frame="true" align="right" spinBox="true"
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'''M2 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 20 STRUCTURES'''<br />
'''M2 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 20 STRUCTURES'''<br />
==Overview==
==Overview==
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A synthetic peptide corresponding to the transmembrane segment M2, (residues 236-267) of the alpha-subunit of the nicotinic acetylcholine, receptor from Torpedo californica has been studied by two dimensional, 1H-NMR spectroscopy in a chloroform-methanol (1:1) mixture containing 0.1, M LiClO4. Reconstruction of the spatial structure of M2 from the NMR data, resulted in an alpha-helix formed by residues 241-263. Distribution of the, molecular hydrophobicity potential on the helix surface is very similar to, that in five-helix bundles of proteins with a known three dimensional, structure: two hydrophilic bands located on the opposite helix sides, separated by strong hydrophobic zones.
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A synthetic peptide corresponding to the transmembrane segment M2 (residues 236-267) of the alpha-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by two dimensional 1H-NMR spectroscopy in a chloroform-methanol (1:1) mixture containing 0.1 M LiClO4. Reconstruction of the spatial structure of M2 from the NMR data resulted in an alpha-helix formed by residues 241-263. Distribution of the molecular hydrophobicity potential on the helix surface is very similar to that in five-helix bundles of proteins with a known three dimensional structure: two hydrophilic bands located on the opposite helix sides separated by strong hydrophobic zones.
==About this Structure==
==About this Structure==
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1DXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DXZ OCA].
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1DXZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DXZ OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Torpedo californica]]
[[Category: Torpedo californica]]
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[[Category: Arseniev, A.S.]]
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[[Category: Arseniev, A S.]]
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[[Category: Efremov, R.G.]]
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[[Category: Efremov, R G.]]
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[[Category: Ivanov, V.T.]]
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[[Category: Ivanov, V T.]]
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[[Category: Maslennikov, I.V.]]
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[[Category: Maslennikov, I V.]]
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[[Category: Pashkov, V.S.]]
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[[Category: Pashkov, V S.]]
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[[Category: Tchikin, L.D.]]
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[[Category: Tchikin, L D.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: ion-channel]]
[[Category: ion-channel]]
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[[Category: transmembrane segment]]
[[Category: transmembrane segment]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:40:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:44 2008''

Revision as of 10:21, 21 February 2008


1dxz

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M2 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 20 STRUCTURES

Overview

A synthetic peptide corresponding to the transmembrane segment M2 (residues 236-267) of the alpha-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by two dimensional 1H-NMR spectroscopy in a chloroform-methanol (1:1) mixture containing 0.1 M LiClO4. Reconstruction of the spatial structure of M2 from the NMR data resulted in an alpha-helix formed by residues 241-263. Distribution of the molecular hydrophobicity potential on the helix surface is very similar to that in five-helix bundles of proteins with a known three dimensional structure: two hydrophilic bands located on the opposite helix sides separated by strong hydrophobic zones.

About this Structure

1DXZ is a Single protein structure of sequence from Torpedo californica with as ligand. Full crystallographic information is available from OCA.

Reference

Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor alpha-subunit., Pashkov VS, Maslennikov IV, Tchikin LD, Efremov RG, Ivanov VT, Arseniev AS, FEBS Lett. 1999 Aug 20;457(1):117-21. PMID:10486576

Page seeded by OCA on Thu Feb 21 12:21:44 2008

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