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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : Doklady. Biochemistry and biophysics

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Doklady. Biochemistry and biophysics - 15 Jul 2016

Faure G, Shelukhina IV, Porowinska D, Shulepko MA, Lyukmanova EN, Dolgikh DA, Spirova EN, Kasheverov IE, Utkin YN, Corringer JP, Tsetlin VI

Link to Pubmed [PMID] – 27417718

Dokl. Biochem. Biophys. 2016 May;468(1):193-6

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.

https://www.ncbi.nlm.nih.gov/pubmed/27417718