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Three-dimensional structure of the alpha-conotoxin EI determined by proton NMR spectroscopy

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Date Issued:
1998
Summary:
The alpha-conotoxin EI is an 18-residue peptide (RDOCCYHPTCNMSNPQIC; 4-10, 5-18) isolated from the venom of Conus ermineus. This peptide targets the nicotinic acetylcholine receptor (nAChR) found in mammalian skeletal muscle and the electric organ of Torpedo. 2D-NMR methods and dynamical simulated annealing protocols have been used to determine the 3D structure of EI. 133 NOE-derived distances were used to produce 13 structures with minimum energy that complied with the NOE restraints. The structure of EI is characterized by a helical loop between T9 and M12 that is stabilized by the C4-C10 disulfide bond and turns involving C4-C5 and N14-P15. The overall fold of EI is similar to that of other alpha4/7 conotoxins (PnIA/B, MII, EpI). However, unlike these other alpha4/7 conotoxins, EI targets the muscular type nAChR. The differences in selectivity can be attributed to the surface charge distribution among these alpha4/7 conotoxins.
Title: Three-dimensional structure of the alpha-conotoxin EI determined by proton NMR spectroscopy.
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Name(s): Franco, Aldo
Florida Atlantic University, Degree Grantor
Mari, Frank, Thesis Advisor
Type of Resource: text
Genre: Electronic Thesis Or Dissertation
Date Issued: 1998
Publisher: Florida Atlantic University
Place of Publication: Boca Raton, Fla.
Physical Form: application/pdf
Extent: 80 p.
Language(s): English
Summary: The alpha-conotoxin EI is an 18-residue peptide (RDOCCYHPTCNMSNPQIC; 4-10, 5-18) isolated from the venom of Conus ermineus. This peptide targets the nicotinic acetylcholine receptor (nAChR) found in mammalian skeletal muscle and the electric organ of Torpedo. 2D-NMR methods and dynamical simulated annealing protocols have been used to determine the 3D structure of EI. 133 NOE-derived distances were used to produce 13 structures with minimum energy that complied with the NOE restraints. The structure of EI is characterized by a helical loop between T9 and M12 that is stabilized by the C4-C10 disulfide bond and turns involving C4-C5 and N14-P15. The overall fold of EI is similar to that of other alpha4/7 conotoxins (PnIA/B, MII, EpI). However, unlike these other alpha4/7 conotoxins, EI targets the muscular type nAChR. The differences in selectivity can be attributed to the surface charge distribution among these alpha4/7 conotoxins.
Identifier: 9780599109230 (isbn), 15609 (digitool), FADT15609 (IID), fau:12367 (fedora)
Note(s): Thesis (M.S.)--Florida Atlantic University, 1998.
Subject(s): Conus--Venom
Peptides--Structure
Nuclear magnetic resonance spectroscopy
Held by: Florida Atlantic University Libraries
Persistent Link to This Record: http://purl.flvc.org/fcla/dt/15609
Sublocation: Digital Library
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Host Institution: FAU
Is Part of Series: Florida Atlantic University Digital Library Collections.