1mxp

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(New page: 200px<br /><applet load="1mxp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mxp" /> '''Solution structure of the ribbon disulfide b...)
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[[Image:1mxp.gif|left|200px]]<br /><applet load="1mxp" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB'''<br />
'''Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB'''<br />
==Overview==
==Overview==
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alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been, synthesized to determine the role of disulfide bond connectivity on, structure and activity. Both of these peptides contain the 15 amino acid, sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the, disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the, disulfide connectivity Cys(2-15 and 3-8). The solution structures of the, peptides were determined by NMR spectroscopy, and their ability to block, the nicotinic acetylcholine receptors on dissociated neurons of the rat, parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to, have approximately 10 times greater potency than the native peptide. To, our knowledge this is the first demonstration of a non-native disulfide, bond isomer of a conotoxin exhibiting greater biological activity than the, native isomer.
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alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been synthesized to determine the role of disulfide bond connectivity on structure and activity. Both of these peptides contain the 15 amino acid sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the disulfide connectivity Cys(2-15 and 3-8). The solution structures of the peptides were determined by NMR spectroscopy, and their ability to block the nicotinic acetylcholine receptors on dissociated neurons of the rat parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to have approximately 10 times greater potency than the native peptide. To our knowledge this is the first demonstration of a non-native disulfide bond isomer of a conotoxin exhibiting greater biological activity than the native isomer.
==About this Structure==
==About this Structure==
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1MXP 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=1MXP OCA].
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1MXP 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=1MXP OCA].
==Reference==
==Reference==
A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity., Dutton JL, Bansal PS, Hogg RC, Adams DJ, Alewood PF, Craik DJ, J Biol Chem. 2002 Dec 13;277(50):48849-57. Epub 2002 Oct 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12376538 12376538]
A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity., Dutton JL, Bansal PS, Hogg RC, Adams DJ, Alewood PF, Craik DJ, J Biol Chem. 2002 Dec 13;277(50):48849-57. Epub 2002 Oct 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12376538 12376538]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Adams, D.J.]]
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[[Category: Adams, D J.]]
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[[Category: Alewood, P.F.]]
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[[Category: Alewood, P F.]]
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[[Category: Bansal, P.S.]]
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[[Category: Bansal, P S.]]
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[[Category: Craik, D.J.]]
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[[Category: Craik, D J.]]
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[[Category: Dutton, J.L.]]
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[[Category: Dutton, J L.]]
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[[Category: Hogg, R.C.]]
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[[Category: Hogg, R C.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: turns]]
[[Category: turns]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:47:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:07 2008''

Revision as of 12:00, 21 February 2008


1mxp

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Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB

Overview

alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been synthesized to determine the role of disulfide bond connectivity on structure and activity. Both of these peptides contain the 15 amino acid sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the disulfide connectivity Cys(2-15 and 3-8). The solution structures of the peptides were determined by NMR spectroscopy, and their ability to block the nicotinic acetylcholine receptors on dissociated neurons of the rat parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to have approximately 10 times greater potency than the native peptide. To our knowledge this is the first demonstration of a non-native disulfide bond isomer of a conotoxin exhibiting greater biological activity than the native isomer.

About this Structure

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

Reference

A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity., Dutton JL, Bansal PS, Hogg RC, Adams DJ, Alewood PF, Craik DJ, J Biol Chem. 2002 Dec 13;277(50):48849-57. Epub 2002 Oct 9. PMID:12376538

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