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Interaction of three-finger proteins from snake venoms and from mammalian brain with the cys-loop receptors and their models

Abstract : With the use of surface plasmon resonance (SPR) it was shown that ws-Lynx1, a water-soluble analog of the three-finger membrane-bound protein Lynx1, that modulates the activity of brain nicotinic acetylcholine receptors (nAChRs), interacts with the acetylcholine-binding protein (AChBP) with high affinity, K D = 62 nM. This result agrees with the earlier demonstrated competition of ws-Lynx1 with radioiodinated α-bungarotoxin for binding to AChBP. For the first time it was shown that ws-Lynx1 binds to GLIC, prokaryotic Cys-loop receptor (K D = 1.3 μM). On the contrary, SPR revealed that α-cobratoxin, a three-finger protein from cobra venom, does not bind to GLIC. Obtained results indicate that SPR is a promising method for analysis of topography of ws-Lynx1 binding sites using its mutants and those of AChBP and GLIC.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-01721253
Contributor : Ana Cova Rodrigues <>
Submitted on : Thursday, March 1, 2018 - 7:36:29 PM
Last modification on : Tuesday, July 14, 2020 - 11:04:07 AM

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G. Faure, V. Shelukhina, Dorota Porowinska, M. Shulepko, E. Lyukmanova, et al.. Interaction of three-finger proteins from snake venoms and from mammalian brain with the cys-loop receptors and their models. Доклады Академии Наук / Doklady Biochemistry and Biophysics, MAIK Nauka/Interperiodica, 2016, 468 (1), pp.193 - 196. ⟨10.1134/S1607672916030091⟩. ⟨pasteur-01721253⟩

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