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New page: left|200px<br /><applet load="2i28" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i28" /> '''Solution Structure of alpha-Conotoxin BuIA''...
 
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[[Image:2i28.jpg|left|200px]]<br /><applet load="2i28" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2i28.jpg|left|200px]]<br /><applet load="2i28" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2i28" />
caption="2i28" />
'''Solution Structure of alpha-Conotoxin BuIA'''<br />
'''Solution Structure of alpha-Conotoxin BuIA'''<br />


==Overview==
==Overview==
We have determined a high-resolution three-dimensional structure of, alpha-conotoxin BuIA, a 13-residue peptide toxin isolated from Conus, bullatus. Despite its unusual 4/4 disulfide bond layout alpha-conotoxin, BuIA exhibits strong antagonistic activity at alpha6/alpha3beta2beta3, alpha3beta2, and alpha3beta4 nAChR subtypes like some alpha4/7 conotoxins., alpha-Conotoxin BuIA lacks the C-terminal beta-turn present within the, second disulfide loop of alpha4/7 conotoxins, having only a "pseudo, omega-shaped" molecular topology. Nevertheless, it contains a functionally, critical two-turn helix motif, a feature ubiquitously found in alpha4/7, conotoxins. Such an aspect seems mainly responsible for similarities in, the receptor recognition profile of alpha-conotoxin BuIA to alpha4/7, conotoxins. Structural comparison of alpha-conotoxin BuIA with alpha4/7, conotoxins and alpha4/3 conotoxin ImI suggests that presence of the second, helical turn portion of the two-turn helix motif in alpha4/7 and alpha4/4, conotoxins may be important for binding to the alpha3 and/or alpha6, subunit of nAChR.
We have determined a high-resolution three-dimensional structure of alpha-conotoxin BuIA, a 13-residue peptide toxin isolated from Conus bullatus. Despite its unusual 4/4 disulfide bond layout alpha-conotoxin BuIA exhibits strong antagonistic activity at alpha6/alpha3beta2beta3, alpha3beta2, and alpha3beta4 nAChR subtypes like some alpha4/7 conotoxins. alpha-Conotoxin BuIA lacks the C-terminal beta-turn present within the second disulfide loop of alpha4/7 conotoxins, having only a "pseudo omega-shaped" molecular topology. Nevertheless, it contains a functionally critical two-turn helix motif, a feature ubiquitously found in alpha4/7 conotoxins. Such an aspect seems mainly responsible for similarities in the receptor recognition profile of alpha-conotoxin BuIA to alpha4/7 conotoxins. Structural comparison of alpha-conotoxin BuIA with alpha4/7 conotoxins and alpha4/3 conotoxin ImI suggests that presence of the second helical turn portion of the two-turn helix motif in alpha4/7 and alpha4/4 conotoxins may be important for binding to the alpha3 and/or alpha6 subunit of nAChR.


==About this Structure==
==About this Structure==
2I28 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=2I28 OCA].  
2I28 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=2I28 OCA].  


==Reference==
==Reference==
NMR structure determination of alpha-conotoxin BuIA, a novel neuronal nicotinic acetylcholine receptor antagonist with an unusual 4/4 disulfide scaffold., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2006 Nov 3;349(4):1228-34. Epub 2006 Sep 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16979596 16979596]
NMR structure determination of alpha-conotoxin BuIA, a novel neuronal nicotinic acetylcholine receptor antagonist with an unusual 4/4 disulfide scaffold., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2006 Nov 3;349(4):1228-34. Epub 2006 Sep 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16979596 16979596]
[[Category: Single protein]]
[[Category: Single protein]]
[[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]]
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[[Category: two disulfide bonds]]
[[Category: two disulfide bonds]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:06:47 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:17 2008''

Revision as of 15:48, 21 February 2008

File:2i28.jpg


2i28

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Solution Structure of alpha-Conotoxin BuIA

Overview

We have determined a high-resolution three-dimensional structure of alpha-conotoxin BuIA, a 13-residue peptide toxin isolated from Conus bullatus. Despite its unusual 4/4 disulfide bond layout alpha-conotoxin BuIA exhibits strong antagonistic activity at alpha6/alpha3beta2beta3, alpha3beta2, and alpha3beta4 nAChR subtypes like some alpha4/7 conotoxins. alpha-Conotoxin BuIA lacks the C-terminal beta-turn present within the second disulfide loop of alpha4/7 conotoxins, having only a "pseudo omega-shaped" molecular topology. Nevertheless, it contains a functionally critical two-turn helix motif, a feature ubiquitously found in alpha4/7 conotoxins. Such an aspect seems mainly responsible for similarities in the receptor recognition profile of alpha-conotoxin BuIA to alpha4/7 conotoxins. Structural comparison of alpha-conotoxin BuIA with alpha4/7 conotoxins and alpha4/3 conotoxin ImI suggests that presence of the second helical turn portion of the two-turn helix motif in alpha4/7 and alpha4/4 conotoxins may be important for binding to the alpha3 and/or alpha6 subunit of nAChR.

About this Structure

2I28 is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.

Reference

NMR structure determination of alpha-conotoxin BuIA, a novel neuronal nicotinic acetylcholine receptor antagonist with an unusual 4/4 disulfide scaffold., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem Biophys Res Commun. 2006 Nov 3;349(4):1228-34. Epub 2006 Sep 7. PMID:16979596

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