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Journal articles
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-01721253
Contributor : Ana Cova Rodrigues Connect in order to contact the contributor
Submitted on : Thursday, March 1, 2018 - 7:36:29 PM
Last modification on : Wednesday, November 3, 2021 - 9:16:18 AM
Contributor : Ana Cova Rodrigues Connect in order to contact the contributor
Submitted on : Thursday, March 1, 2018 - 7:36:29 PM
Last modification on : Wednesday, November 3, 2021 - 9:16:18 AM