2czp
From Proteopedia
(New page: 200px<br /><applet load="2czp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2czp" /> '''Structural analysis of membrane-bound mastop...) |
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| - | [[Image:2czp.gif|left|200px]]<br /><applet load="2czp" size=" | + | [[Image:2czp.gif|left|200px]]<br /><applet load="2czp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2czp" /> | caption="2czp" /> | ||
'''Structural analysis of membrane-bound mastoparan-X by solid-state NMR'''<br /> | '''Structural analysis of membrane-bound mastoparan-X by solid-state NMR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of mastoparan-X (MP-X), a G-protein activating peptide from | + | The structure of mastoparan-X (MP-X), a G-protein activating peptide from wasp venom, in the state tightly bound to anionic phospholipid bilayers was determined by solid-state NMR spectroscopy. Carbon-13 and nitrogen-15 NMR signals of uniformly labeled MP-X were completely assigned by multidimensional intraresidue C-C, N-CalphaCbeta, and N-Calpha-C', and interresidue Calpha-CalphaCbeta, N-CalphaCbeta, and N-C'-Calpha correlation experiments. The backbone torsion angles were predicted from the chemical shifts of 13C', 13Calpha, 13Cbeta, and 15N signals with the aid of protein NMR database programs. In addition, two 13C-13C and three 13C-15N distances between backbone nuclei were precisely measured by rotational resonance and REDOR experiments, respectively. The backbone structure of MP-X was determined from the 26 dihedral angle restraints and five distances with an average root-mean-square deviation of 0.6 A. Peptide MP-X in the bilayer-bound state formed an amphiphilic alpha-helix for residues Trp3-Leu14 and adopted an extended conformation for Asn2. This membrane-bound conformation is discussed in relation to the peptide's activities to form pores in membranes and to activate G-proteins. This study demonstrates the power of multidimensional solid-state NMR of uniformly isotope-labeled molecules and distance measurements for determining the structures of peptides bound to lipid membranes. |
==About this Structure== | ==About this Structure== | ||
| - | 2CZP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vespa_simillima_xanthoptera Vespa simillima xanthoptera] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2CZP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vespa_simillima_xanthoptera Vespa simillima xanthoptera] 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=2CZP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fujiwara, T.]] | [[Category: Fujiwara, T.]] | ||
[[Category: Fukushima, K.]] | [[Category: Fukushima, K.]] | ||
| - | [[Category: Kang, S | + | [[Category: Kang, S W.]] |
[[Category: Kohno, T.]] | [[Category: Kohno, T.]] | ||
| - | [[Category: Park, J | + | [[Category: Park, J S.]] |
[[Category: Todokoro, Y.]] | [[Category: Todokoro, Y.]] | ||
[[Category: Wakamatsu, K.]] | [[Category: Wakamatsu, K.]] | ||
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[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:58 2008'' |
Revision as of 14:54, 21 February 2008
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Structural analysis of membrane-bound mastoparan-X by solid-state NMR
Overview
The structure of mastoparan-X (MP-X), a G-protein activating peptide from wasp venom, in the state tightly bound to anionic phospholipid bilayers was determined by solid-state NMR spectroscopy. Carbon-13 and nitrogen-15 NMR signals of uniformly labeled MP-X were completely assigned by multidimensional intraresidue C-C, N-CalphaCbeta, and N-Calpha-C', and interresidue Calpha-CalphaCbeta, N-CalphaCbeta, and N-C'-Calpha correlation experiments. The backbone torsion angles were predicted from the chemical shifts of 13C', 13Calpha, 13Cbeta, and 15N signals with the aid of protein NMR database programs. In addition, two 13C-13C and three 13C-15N distances between backbone nuclei were precisely measured by rotational resonance and REDOR experiments, respectively. The backbone structure of MP-X was determined from the 26 dihedral angle restraints and five distances with an average root-mean-square deviation of 0.6 A. Peptide MP-X in the bilayer-bound state formed an amphiphilic alpha-helix for residues Trp3-Leu14 and adopted an extended conformation for Asn2. This membrane-bound conformation is discussed in relation to the peptide's activities to form pores in membranes and to activate G-proteins. This study demonstrates the power of multidimensional solid-state NMR of uniformly isotope-labeled molecules and distance measurements for determining the structures of peptides bound to lipid membranes.
About this Structure
2CZP is a Single protein structure of sequence from Vespa simillima xanthoptera with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of tightly membrane-bound mastoparan-X, a G-protein-activating peptide, determined by solid-state NMR., Todokoro Y, Yumen I, Fukushima K, Kang SW, Park JS, Kohno T, Wakamatsu K, Akutsu H, Fujiwara T, Biophys J. 2006 Aug 15;91(4):1368-79. Epub 2006 May 19. PMID:16714348
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