2i28
From Proteopedia
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|PDB= 2i28 |SIZE=350|CAPTION= <scene name='initialview01'>2i28</scene> | |PDB= 2i28 |SIZE=350|CAPTION= <scene name='initialview01'>2i28</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i28 OCA], [http://www.ebi.ac.uk/pdbsum/2i28 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i28 RCSB]</span> | ||
}} | }} | ||
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[[Category: McIntosh, J M.]] | [[Category: McIntosh, J M.]] | ||
[[Category: Olivera, B M.]] | [[Category: Olivera, B M.]] | ||
| - | [[Category: NH2]] | ||
[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
[[Category: beta-turn]] | [[Category: beta-turn]] | ||
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[[Category: two disulfide bond]] | [[Category: two disulfide bond]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:43 2008'' |
Revision as of 00:38, 31 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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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