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

G. Faure (1) , V. Shelukhina (2) , Dorota Porowinska (1, 3) , M. Shulepko (2) , E. Lyukmanova (2) , D. Dolgikh (2) , E. Spirova (2) , I. Kasheverov (2) , Yu. Utkin (2) , Pierre-Jean Corringer (1) , V. I. Tsetlin (2)

1 Récepteurs Canaux - Channel Receptors
2 IBCh RAS - Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
3 Nicolaus Copernicus University [Toruń]

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.

Domaines: Neurosciences

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, 2016, 468 (1), pp.193 - 196. ⟨10.1134/S1607672916030091⟩. ⟨pasteur-01721253⟩