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Mar. Drugs 2016, 14(10), 173; doi:10.3390/md14100173

Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs

1,2
,
3,* and 1,2,*
1
Hainan Provincial Key Laboratory of Carcinogenesis and Intervention, Hainan Medical College, Haikou 571199, Hainan, China
2
Institution of Tumor, Hainan Medical College, Haikou 570102, Hainan, China
3
Nebraska Center for Virology, School of Veterinary Medicine and Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68583, USA
*
Authors to whom correspondence should be addressed.
Academic Editors: John B. MacMillan and Tadeusz F. Molinski
Received: 28 July 2016 / Revised: 20 September 2016 / Accepted: 21 September 2016 / Published: 11 October 2016
(This article belongs to the Special Issue Structural Techniques in Natural Products Drug Discovery)
View Full-Text   |   Download PDF [11147 KB, uploaded 11 October 2016]   |  

Abstract

Nicotinic acetylcholine receptors (nAChRs) are targets for developing new drugs to treat severe pain, nicotine addiction, Alzheimer disease, epilepsy, etc. α-Conotoxins are biologically and chemically diverse. With 12–19 residues and two disulfides, they can be specifically selected for different nAChRs. Acetylcholine-binding proteins from Aplysia californica (Ac-AChBP) are homologous to the ligand-binding domains of nAChRs and pharmacologically similar. X-ray structures of the α-conotoxin in complex with Ac-AChBP in addition to computer modeling have helped to determine the binding site of the important residues of α-conotoxin and its affinity for nAChR subtypes. Here, we present the various α-conotoxin residues that are selective for Ac-AChBP or nAChRs by comparing the structures of α-conotoxins in complex with Ac-AChBP and by modeling α-conotoxins in complex with nAChRs. The knowledge of these binding sites will assist in the discovery and design of more potent and selective α-conotoxins as drug leads. View Full-Text
Keywords: α-conotoxins; nAChRs; Ac-AChBP; X-ray structure; model; design α-conotoxins; nAChRs; Ac-AChBP; X-ray structure; model; design
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MDPI and ACS Style

Lin, B.; Xiang, S.; Li, M. Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs. Mar. Drugs 2016, 14, 173.

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