2czp
From Proteopedia
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| - | + | {{STRUCTURE_2czp| PDB=2czp | SCENE= }} | |
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'''Structural analysis of membrane-bound mastoparan-X by solid-state NMR''' | '''Structural analysis of membrane-bound mastoparan-X by solid-state NMR''' | ||
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[[Category: Yumen, I.]] | [[Category: Yumen, I.]] | ||
[[Category: 3d-structure]] | [[Category: 3d-structure]] | ||
| - | [[Category: | + | [[Category: Amidation]] |
| - | [[Category: | + | [[Category: Mast cell degranulation]] |
| - | [[Category: | + | [[Category: Mastoparan x]] |
| - | [[Category: | + | [[Category: Membrane bound]] |
| - | [[Category: | + | [[Category: Mp-x]] |
| - | [[Category: | + | [[Category: Venom]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:25:38 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:25, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 23:25:38 2008
