1dw5: Difference between revisions

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New page: left|200px<br /><applet load="1dw5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dw5" /> '''NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO C...
 
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[[Image:1dw5.gif|left|200px]]<br /><applet load="1dw5" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dw5.gif|left|200px]]<br /><applet load="1dw5" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dw5" />
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'''NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES'''<br />
'''NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES'''<br />


==Overview==
==Overview==
omega-Conotoxin MVIIA is a 25-residue, disulfide-bridged polypeptide from, the venom of the sea snail Conus magus that binds to neuronal N-type, calcium channels. It forms a compact folded structure, presenting a loop, between Cys8 and Cys15 that contains a set of residues critical for its, binding. The loop does not have a unique defined structure, nor is it, intrinsically flexible. Broadening of a subset of resonances in the NMR, spectrum at low temperature, anomalous temperature dependence of the, chemical shifts of some resonances, and exchange contributions to J(0), from (13)C relaxation measurements reveal that conformational exchange, affects the residues in this loop. The effects of this exchange on the, calculated structure of omega-conotoxin MVIIA are discussed. The exchange, appears to be associated with a change in the conformation of the, disulfide bridge Cys8-Cys20. The implications for the use of the, omega-conotoxins as a scaffold for carrying other functions is discussed.
omega-Conotoxin MVIIA is a 25-residue, disulfide-bridged polypeptide from the venom of the sea snail Conus magus that binds to neuronal N-type calcium channels. It forms a compact folded structure, presenting a loop between Cys8 and Cys15 that contains a set of residues critical for its binding. The loop does not have a unique defined structure, nor is it intrinsically flexible. Broadening of a subset of resonances in the NMR spectrum at low temperature, anomalous temperature dependence of the chemical shifts of some resonances, and exchange contributions to J(0) from (13)C relaxation measurements reveal that conformational exchange affects the residues in this loop. The effects of this exchange on the calculated structure of omega-conotoxin MVIIA are discussed. The exchange appears to be associated with a change in the conformation of the disulfide bridge Cys8-Cys20. The implications for the use of the omega-conotoxins as a scaffold for carrying other functions is discussed.


==About this Structure==
==About this Structure==
1DW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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=1DW5 OCA].  
1DW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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=1DW5 OCA].  


==Reference==
==Reference==
Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange., Atkinson RA, Kieffer B, Dejaegere A, Sirockin F, Lefevre JF, Biochemistry. 2000 Apr 11;39(14):3908-19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10747778 10747778]
Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange., Atkinson RA, Kieffer B, Dejaegere A, Sirockin F, Lefevre JF, Biochemistry. 2000 Apr 11;39(14):3908-19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10747778 10747778]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Atkinson, R.A.]]
[[Category: Atkinson, R A.]]
[[Category: Dejaegere, A.]]
[[Category: Dejaegere, A.]]
[[Category: Kieffer, B.]]
[[Category: Kieffer, B.]]
[[Category: Lefevre, J.F.]]
[[Category: Lefevre, J F.]]
[[Category: Sirockin, F.]]
[[Category: Sirockin, F.]]
[[Category: NH2]]
[[Category: NH2]]
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[[Category: conotoxin]]
[[Category: conotoxin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:38:12 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:07 2008''

Revision as of 13:21, 21 February 2008

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1dw5

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NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES

OverviewOverview

omega-Conotoxin MVIIA is a 25-residue, disulfide-bridged polypeptide from the venom of the sea snail Conus magus that binds to neuronal N-type calcium channels. It forms a compact folded structure, presenting a loop between Cys8 and Cys15 that contains a set of residues critical for its binding. The loop does not have a unique defined structure, nor is it intrinsically flexible. Broadening of a subset of resonances in the NMR spectrum at low temperature, anomalous temperature dependence of the chemical shifts of some resonances, and exchange contributions to J(0) from (13)C relaxation measurements reveal that conformational exchange affects the residues in this loop. The effects of this exchange on the calculated structure of omega-conotoxin MVIIA are discussed. The exchange appears to be associated with a change in the conformation of the disulfide bridge Cys8-Cys20. The implications for the use of the omega-conotoxins as a scaffold for carrying other functions is discussed.

About this StructureAbout this Structure

1DW5 is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange., Atkinson RA, Kieffer B, Dejaegere A, Sirockin F, Lefevre JF, Biochemistry. 2000 Apr 11;39(14):3908-19. PMID:10747778

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