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Title 

Solution conformation of α-conotoxin GIC, a novel potent antagonist of α3β2 nicotinic acetylcholine receptors

Authors 

Seung-Wook ChiDo-Hyoung KimB M OliveraJ M McIntoshKyou Hoon Han

Publisher 

Portland Press

Issue Date 

2004

Citation 

Biochemical Journal, vol. 380, no. 2, pp. 347-352

Keywords 

α-conotoxinconus geographus (cone snail)nicotinic acetylcholine receptor (nAChR)NMRsolution structurevenomchemical bondsnuclear magnetic resonance spectroscopytoxic materialsacetylcholine

Abstract 

α-Conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. α-Conotoxin GIC potently blocks the α3β2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution structure of α-conotoxin GIC by NMR spectroscopy. The structure of α-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2-16) of 0.53 ? and 0.96 ? respectively. Structure and surface comparison of α-conotoxin GIC with the other α4/7 subfamily conotoxins reveals unique structural aspects of α-conotoxin GIC. In particular, the structural comparison between α-conotoxins GIC and MII indicates molecular features that may confer their similar receptor specificity profile, as well as those that provide the unique binding characteristics of α-conotoxin GIC.

ISSN 

0264-6021

Link 

http://dx.doi.org/10.1042/BJ20031792

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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