Structure-functional intimacies of transient receptor potential channels.

@article{Latorre2009StructurefunctionalIO,
  title={Structure-functional intimacies of transient receptor potential channels.},
  author={Ram{\'o}n Latorre and Cristi{\'a}n Zaelzer and Sebasti{\'a}n Brauchi},
  journal={Quarterly reviews of biophysics},
  year={2009},
  volume={42 3},
  pages={
          201-46
        }
}
Although a unifying characteristic common to all transient receptor potential (TRP) channel functions remains elusive, they could be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. TRP channels constitute a large superfamily of ion channels, and can be grouped into seven subfamilies based on their amino acid sequence homology: the canonical or classic TRPs, the vanilloid… CONTINUE READING
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