1a0m: Difference between revisions
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|PDB= 1a0m |SIZE=350|CAPTION= <scene name='initialview01'>1a0m</scene>, resolution 1.1Å | |PDB= 1a0m |SIZE=350|CAPTION= <scene name='initialview01'>1a0m</scene>, resolution 1.1Å | ||
|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=1a0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a0m OCA], [http://www.ebi.ac.uk/pdbsum/1a0m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a0m RCSB]</span> | |||
}} | }} | ||
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[[Category: Miller, R.]] | [[Category: Miller, R.]] | ||
[[Category: Weeks, C M.]] | [[Category: Weeks, C M.]] | ||
[[Category: a-conotoxin]] | [[Category: a-conotoxin]] | ||
[[Category: acetylcholine receptor antagonist]] | [[Category: acetylcholine receptor antagonist]] | ||
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[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:30:35 2008'' | ||
Revision as of 18:30, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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