Direct Gating of ATP-activated Ion Channels (P2X2 Receptors) by Lipophilic Attachment at the Outer End of the Second Transmembrane Domain

The ionic pore of the P2X receptor passes through the central axis of six transmembrane (TM) helices, two from each of three subunits. Val(48) and Ile(328) are at the outer end of TM1 and TM2, respectively. Homology models of the open and closed states of P2X2 indicate that pore opening is associate...

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Detalles Bibliográficos
Autores principales: Rothwell, Simon W., Stansfeld, Phillip J., Bragg, Laricia, Verkhratsky, Alexej, North, R. Alan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2014
Materias:
Molecular Biophysics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887190/
https://www.ncbi.nlm.nih.gov/pubmed/24273165
http://dx.doi.org/10.1074/jbc.M113.529099

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3887190/
https://www.ncbi.nlm.nih.gov/pubmed/24273165
http://dx.doi.org/10.1074/jbc.M113.529099

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