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  • The 1.1 Å Resolution crystal structure of [Tyr15]EpI, a novel a-Conotoxin from Conus episcopatus, solved by direct methods

    Author
    Hu, Shu-Hong
    Loughnan, Marion L.
    Miller, Russ
    Weeks, Charles M.
    Blessing, Robert H.
    Alewood, Paul F.
    Lewis, Richard J.
    Martin, Jennifer L.
    Year published
    1998
    Metadata
    Show full item record
    Abstract
    Conotoxins are valuable probes of receptors and ion channels because of their small size and highly selective activity. α-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 α3β2 and α3β4 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 Å using SnB. The asymmetric ...
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    Conotoxins are valuable probes of receptors and ion channels because of their small size and highly selective activity. α-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 α3β2 and α3β4 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 Å 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 α-conotoxin structures that have been determined to date. Four of these, [Tyr15]EpI, PnIA, PnIB, and MII, have an α4/7 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 α4/7-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.
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    Journal Title
    Biochemistry
    Volume
    37
    Issue
    33
    DOI
    https://doi.org/10.1021/bi9806549
    Subject
    Biochemistry and Cell Biology not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/347899
    Collection
    • Journal articles

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