Title : Rational design and validation of a vanilloid-sensitive TRPV2 ion channel.

Pub. Date : 2016 Jun 28

PMID : 27298359






4 Functional Relationships(s)
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1 Based on these new findings, here we have successfully introduced high-affinity binding of capsaicin and resiniferatoxin to the vanilloid-insensitive TRPV2 channel, using a rationally designed minimal set of four point mutations (F467S-S498F-L505T-Q525E, termed TRPV2_Quad). resiniferatoxin transient receptor potential cation channel subfamily V member 2 Homo sapiens
2 Based on these new findings, here we have successfully introduced high-affinity binding of capsaicin and resiniferatoxin to the vanilloid-insensitive TRPV2 channel, using a rationally designed minimal set of four point mutations (F467S-S498F-L505T-Q525E, termed TRPV2_Quad). resiniferatoxin transient receptor potential cation channel subfamily V member 2 Homo sapiens
3 We found that binding of resiniferatoxin activates TRPV2_Quad but the ligand-induced open state is relatively unstable, whereas binding of capsaicin to TRPV2_Quad antagonizes resiniferatoxin-induced activation likely through competition for the same binding sites. resiniferatoxin transient receptor potential cation channel subfamily V member 2 Homo sapiens
4 We found that binding of resiniferatoxin activates TRPV2_Quad but the ligand-induced open state is relatively unstable, whereas binding of capsaicin to TRPV2_Quad antagonizes resiniferatoxin-induced activation likely through competition for the same binding sites. resiniferatoxin transient receptor potential cation channel subfamily V member 2 Homo sapiens