1UL2

Solution Conformation of alpha-Conotoxin GIC

Summary for 1UL2

• Entry DOI: 10.2210/pdb1ul2/pdb
• NMR Information: BMRB: 5985
• Descriptor: alpha-conotoxin GIC (1 entity in total)
• Functional Keywords: alpha-helix, beta-turn, two disulfide bonds, c-terminal amidation, toxin
• Cellular location: Secreted: Q86RB2
• Total number of polymer chains: 1
• Total formula weight: 1614.83

Authors

Chi, S.-W.,Kim, D.-H.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. (deposition date: 2003-09-06, release date: 2004-07-20, Last modification date: 2024-11-20)

Primary citation

Chi, S.-W.,Kim, D.-H.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H.
Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors
Biochem.J., 380:347-352, 2004

PubMed Abstract: Alpha-conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. Alpha-conotoxin GIC potently blocks the alpha3beta2 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 alpha-conotoxin GIC by NMR spectroscopy. The structure of alpha-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2-16) of 0.53 A and 0.96 A respectively. Structure and surface comparison of alpha-conotoxin GIC with the other alpha4/7 subfamily conotoxins reveals unique structural aspects of alpha-conotoxin GIC. In particular, the structural comparison between alpha-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 alpha-conotoxin GIC.

PubMed: 14992691
DOI: 10.1042/BJ20031792

Experimental method

SOLUTION NMR