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New page: left|200px<br /><applet load="2gcz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gcz" /> '''Solution Structure of alpha-Conotoxin OmIA''...
 
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[[Image:2gcz.gif|left|200px]]<br /><applet load="2gcz" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2gcz.gif|left|200px]]<br /><applet load="2gcz" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2gcz" />
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'''Solution Structure of alpha-Conotoxin OmIA'''<br />
'''Solution Structure of alpha-Conotoxin OmIA'''<br />


==Overview==
==Overview==
alpha-Conotoxin OmIA from Conus omaria is the only alpha-conotoxin that, shows a approximately 20-fold higher affinity to the alpha3beta2 over the, alpha6beta2 subtype of nicotinic acetylcholine receptor. We have, determined a three-dimensional structure of alpha-conotoxin OmIA by, nuclear magnetic resonance spectroscopy. alpha-Conotoxin OmIA has an, "omega-shaped" overall topology with His(5)-Asn(12) forming an, alpha-helix. Structural features of alpha-conotoxin OmIA responsible for, its selectivity are suggested by comparing its surface characteristics, with other functionally related alpha4/7 subfamily conotoxins. Reduced, size of the hydrophilic area in alpha-conotoxin OmIA seems to be, associated with the reduced affinity towards the alpha6beta2 nAChR, subtype.
alpha-Conotoxin OmIA from Conus omaria is the only alpha-conotoxin that shows a approximately 20-fold higher affinity to the alpha3beta2 over the alpha6beta2 subtype of nicotinic acetylcholine receptor. We have determined a three-dimensional structure of alpha-conotoxin OmIA by nuclear magnetic resonance spectroscopy. alpha-Conotoxin OmIA has an "omega-shaped" overall topology with His(5)-Asn(12) forming an alpha-helix. Structural features of alpha-conotoxin OmIA responsible for its selectivity are suggested by comparing its surface characteristics with other functionally related alpha4/7 subfamily conotoxins. Reduced size of the hydrophilic area in alpha-conotoxin OmIA seems to be associated with the reduced affinity towards the alpha6beta2 nAChR subtype.


==About this Structure==
==About this Structure==
2GCZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2GCZ OCA].  
2GCZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2GCZ OCA].  


==Reference==
==Reference==
Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist alpha-conotoxin OmIA that discriminates alpha3 vs. alpha6 nAChR subtypes., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2006 Jun 23;345(1):248-54. Epub 2006 Apr 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16678128 16678128]
Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist alpha-conotoxin OmIA that discriminates alpha3 vs. alpha6 nAChR subtypes., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2006 Jun 23;345(1):248-54. Epub 2006 Apr 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16678128 16678128]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Chi, S.W.]]
[[Category: Chi, S W.]]
[[Category: Han, K.H.]]
[[Category: Han, K H.]]
[[Category: Kim, D.H.]]
[[Category: Kim, D H.]]
[[Category: McIntosh, J.M.]]
[[Category: McIntosh, J M.]]
[[Category: Olivera, B.M.]]
[[Category: Olivera, B M.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: alpha-helix]]
[[Category: alpha-helix]]
Line 23: Line 23:
[[Category: two disulfide bonds]]
[[Category: two disulfide bonds]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:07:52 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:29 2008''

Revision as of 15:30, 21 February 2008

File:2gcz.gif


2gcz

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Solution Structure of alpha-Conotoxin OmIA

Overview

alpha-Conotoxin OmIA from Conus omaria is the only alpha-conotoxin that shows a approximately 20-fold higher affinity to the alpha3beta2 over the alpha6beta2 subtype of nicotinic acetylcholine receptor. We have determined a three-dimensional structure of alpha-conotoxin OmIA by nuclear magnetic resonance spectroscopy. alpha-Conotoxin OmIA has an "omega-shaped" overall topology with His(5)-Asn(12) forming an alpha-helix. Structural features of alpha-conotoxin OmIA responsible for its selectivity are suggested by comparing its surface characteristics with other functionally related alpha4/7 subfamily conotoxins. Reduced size of the hydrophilic area in alpha-conotoxin OmIA seems to be associated with the reduced affinity towards the alpha6beta2 nAChR subtype.

About this Structure

2GCZ is a Protein complex structure of sequences from [1] with NH2 as ligand. Full crystallographic information is available from OCA.

Reference

Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist alpha-conotoxin OmIA that discriminates alpha3 vs. alpha6 nAChR subtypes., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2006 Jun 23;345(1):248-54. Epub 2006 Apr 27. PMID:16678128

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