2gcz: Difference between revisions

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[[~~Image~~:2gcz.~~png|left|200px~~]]

==Solution Structure of alpha-Conotoxin OmIA==

== Structural highlights ==

<table><tr><td colspan='2'>[[2gcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GCZ FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gcz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gcz RCSB], [http://www.ebi.ac.uk/pdbsum/2gcz PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

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.

~~{{STRUCTURE_2gcz| PDB=2gcz | SCENE= }}~~

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<ref>PMID:16678128</ref>

~~===Solution Structure~~ of ~~alpha-Conotoxin OmIA===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_16678128}}~~

== References ==

==~~About this Structure~~==

__TOC__

~~[[2gcz]] is a 1 chain structure. Full experimental information is available from [http:~~//~~oca.weizmann.ac.il/oca-bin/ocashort?id=2GCZ OCA].~~

</StructureSection>

[[Category: Chi, S W.]]

[[Category: Han, K H.]]

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-[[Image:2gcz.png|left|200px]]
+==Solution Structure of alpha-Conotoxin OmIA==
+<StructureSection load='2gcz' size='340' side='right' caption='[[2gcz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2gcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GCZ FirstGlance]. <br>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gcz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gcz RCSB], [http://www.ebi.ac.uk/pdbsum/2gcz PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-{{STRUCTURE_2gcz|  PDB=2gcz  |  SCENE=  }}
+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<ref>PMID:16678128</ref>
-===Solution Structure of alpha-Conotoxin OmIA===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_16678128}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[2gcz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCZ OCA].
+</StructureSection>
 [[Category: Chi, S W.]]
 [[Category: Han, K H.]]