1a0m: Difference between revisions
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'''1.1 ANGSTROM CRYSTAL STRUCTURE OF A-CONOTOXIN [TYR15]-EPI''' | {{Structure | ||
|PDB= 1a0m |SIZE=350|CAPTION= <scene name='initialview01'>1a0m</scene>, resolution 1.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
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'''1.1 ANGSTROM CRYSTAL STRUCTURE OF A-CONOTOXIN [TYR15]-EPI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A0M is a [ | 1A0M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_episcopatus Conus episcopatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0M OCA]. | ||
==Reference== | ==Reference== | ||
The 1.1 A resolution crystal structure of [Tyr15]EpI, a novel alpha-conotoxin from Conus episcopatus, solved by direct methods., Hu SH, Loughnan M, Miller R, Weeks CM, Blessing RH, Alewood PF, Lewis RJ, Martin JL, Biochemistry. 1998 Aug 18;37(33):11425-33. PMID:[http:// | The 1.1 A resolution crystal structure of [Tyr15]EpI, a novel alpha-conotoxin from Conus episcopatus, solved by direct methods., Hu SH, Loughnan M, Miller R, Weeks CM, Blessing RH, Alewood PF, Lewis RJ, Martin JL, Biochemistry. 1998 Aug 18;37(33):11425-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9708977 9708977] | ||
[[Category: Conus episcopatus]] | [[Category: Conus episcopatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:12 2008'' | ||
Revision as of 10:51, 20 March 2008
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1.1 ANGSTROM CRYSTAL STRUCTURE OF A-CONOTOXIN [TYR15]-EPI
OverviewOverview
Conotoxins are valuable probes of receptors and ion channels because of their small size and highly selective activity. alpha-Conotoxin EpI, a 16-residue peptide from the mollusk-hunting Conus episcopatus, has the amino acid sequence GCCSDPRCNMNNPDY(SO3H)C-NH2 and appears to be an extremely potent and selective inhibitor of the alpha3beta2 and alpha3beta4 neuronal subtypes of the nicotinic acetylcholine receptor (nAChR). The desulfated form of EpI ([Tyr15]EpI) has a potency and selectivity for the nAChR receptor similar to those of EpI. Here we describe the crystal structure of [Tyr15]EpI solved at a resolution of 1.1 A using SnB. The asymmetric unit has a total of 284 non-hydrogen atoms, making this one of the largest structures solved de novo by direct methods. The [Tyr15]EpI structure brings to six the number of alpha-conotoxin structures that have been determined to date. Four of these, [Tyr15]EpI, PnIA, PnIB, and MII, have an alpha4/7 cysteine framework and are selective for the neuronal subtype of the nAChR. The structure of [Tyr15]EpI has the same backbone fold as the other alpha4/7-conotoxin structures, supporting the notion that this conotoxin cysteine framework and spacing give rise to a conserved fold. The surface charge distribution of [Tyr15]EpI is similar to that of PnIA and PnIB but is likely to be different from that of MII, suggesting that [Tyr15]EpI and MII may have different binding modes for the same receptor subtype.
About this StructureAbout this Structure
1A0M is a Single protein structure of sequence from Conus episcopatus. Full crystallographic information is available from OCA.
ReferenceReference
The 1.1 A resolution crystal structure of [Tyr15]EpI, a novel alpha-conotoxin from Conus episcopatus, solved by direct methods., Hu SH, Loughnan M, Miller R, Weeks CM, Blessing RH, Alewood PF, Lewis RJ, Martin JL, Biochemistry. 1998 Aug 18;37(33):11425-33. PMID:9708977
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