1a0m: Difference between revisions

Revision as of 15:44, 30 June 2008

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File:1a0m.png

Template:STRUCTURE 1a0m

1.1 ANGSTROM CRYSTAL STRUCTURE OF A-CONOTOXIN [TYR15]-EPI1.1 ANGSTROM CRYSTAL STRUCTURE OF A-CONOTOXIN [TYR15]-EPI

Template:ABSTRACT PUBMED 9708977

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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-'''1.1 ANGSTROM CRYSTAL STRUCTURE OF A-CONOTOXIN [TYR15]-EPI'''
+===1.1 ANGSTROM CRYSTAL STRUCTURE OF A-CONOTOXIN [TYR15]-EPI===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9708977}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9708977 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9708977}}
 ==About this Structure==
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 [[Category: Crystal structure]]
 [[Category: Neurotoxin]]
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