1as5
From Proteopedia
(New page: 200px<br /><applet load="1as5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1as5" /> '''SOLUTION STRUCTURE OF CONOTOXIN Y-PIIIE FROM...) |
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| - | [[Image:1as5.gif|left|200px]]<br /><applet load="1as5" size=" | + | [[Image:1as5.gif|left|200px]]<br /><applet load="1as5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1as5" /> | caption="1as5" /> | ||
'''SOLUTION STRUCTURE OF CONOTOXIN Y-PIIIE FROM CONUS PURPURASCENS, NMR, 14 STRUCTURES'''<br /> | '''SOLUTION STRUCTURE OF CONOTOXIN Y-PIIIE FROM CONUS PURPURASCENS, NMR, 14 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of conotoxin psi-PIIIE, a 24-amino acid | + | The three-dimensional structure of conotoxin psi-PIIIE, a 24-amino acid peptide from Conus purpurascens, has been solved using two-dimensional (2D) 1H NMR spectroscopy. Conotoxin psi-PIIIE contains the same disulfide bonding pattern as the mu-conotoxins, which target skeletal muscle sodium channels, but has been shown to antagonize the acetylcholine gated cation channel through a noncompetitive mechanism. Structural information was obtained by the analysis of a series of 2D NOESY spectra as well as measurement of coupling constants from 1D 1H and PE-COSY NMR experiments. Molecular modeling calculations included the use of the distance geometry (DG) algorithm, simulated annealing techniques, and the restrained molecular dynamics method. The resulting structures are considerably similar to the previously published structures for the mu-conotoxins GIIIA and GIIIB, despite the lack of sequence conservation between conotoxin psi-PIIIE and the mu-conotoxins. The structure consists of a series of tight turns, each turn occurring in the position analogous to those of turns described in mu-GIIIA and mu-GIIIB. This suggests the disulfide bonding pattern is able to largely direct the structure of the peptides, creating a stable structural motif which allows extensive sequence substitution of non-cystine residues. |
==About this Structure== | ==About this Structure== | ||
| - | 1AS5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_purpurascens Conus purpurascens] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1AS5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_purpurascens Conus purpurascens] 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=1AS5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Conus purpurascens]] | [[Category: Conus purpurascens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Foster, M | + | [[Category: Foster, M P.]] |
| - | [[Category: Ireland, C | + | [[Category: Ireland, C M.]] |
| - | [[Category: Mitchell, S | + | [[Category: Mitchell, S S.]] |
| - | [[Category: Olivera, B | + | [[Category: Olivera, B M.]] |
[[Category: Shon, K.]] | [[Category: Shon, K.]] | ||
[[Category: NH2]] | [[Category: NH2]] | ||
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[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:43 2008'' |
Revision as of 09:47, 21 February 2008
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SOLUTION STRUCTURE OF CONOTOXIN Y-PIIIE FROM CONUS PURPURASCENS, NMR, 14 STRUCTURES
Overview
The three-dimensional structure of conotoxin psi-PIIIE, a 24-amino acid peptide from Conus purpurascens, has been solved using two-dimensional (2D) 1H NMR spectroscopy. Conotoxin psi-PIIIE contains the same disulfide bonding pattern as the mu-conotoxins, which target skeletal muscle sodium channels, but has been shown to antagonize the acetylcholine gated cation channel through a noncompetitive mechanism. Structural information was obtained by the analysis of a series of 2D NOESY spectra as well as measurement of coupling constants from 1D 1H and PE-COSY NMR experiments. Molecular modeling calculations included the use of the distance geometry (DG) algorithm, simulated annealing techniques, and the restrained molecular dynamics method. The resulting structures are considerably similar to the previously published structures for the mu-conotoxins GIIIA and GIIIB, despite the lack of sequence conservation between conotoxin psi-PIIIE and the mu-conotoxins. The structure consists of a series of tight turns, each turn occurring in the position analogous to those of turns described in mu-GIIIA and mu-GIIIB. This suggests the disulfide bonding pattern is able to largely direct the structure of the peptides, creating a stable structural motif which allows extensive sequence substitution of non-cystine residues.
About this Structure
1AS5 is a Single protein structure of sequence from Conus purpurascens with as ligand. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure of conotoxin psi-PIIIE, an acetylcholine gated ion channel antagonist., Mitchell SS, Shon KJ, Foster MP, Davis DR, Olivera BM, Ireland CM, Biochemistry. 1998 Feb 3;37(5):1215-20. PMID:9477946
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