Perspectives of TRPV1 Function on the Neurogenesis and Neural Plasticity

Figure 1

Diagram of regions involved in TRPV1 function. (a) The primary structure involves six transmembrane segments (S1–S6) with a pore domain between the fifth (S5) and sixth (S6) segment, and both C and N termini are located intracellularly. The functional TRPV1 receptor is believed to form a homotetramer. Amino acid residues involved in the binding of chemical and physical activation/modulation of TRPV1 activity are indicated in a color scheme. Vanilloid compounds, as the activators capsaicin and resiniferatoxin, as well as inhibitor capsazepine share the same binding site, while cholesterol-binding site is composed of a promiscuous hydrophobic pocket in S5. (b) Model for hydrophobic pocket in S5 linker with the binding of lipidic molecules such as cholesterol (chol), PIP₂, and capsaicin (CAP) generated by molecular dynamics. In this binding conformation, all the molecules occupy a groove formed between S5 and C-terminal of the subunit.

(a)

(b)