Fig. 1: The TRPV structure and its pore on the example of rat TRPV1.
From: Dynamic molecular portraits of ion-conducting pores characterize functional states of TRPV channels
a – The homotetramer of rat TRPV1 (PDB ID 7L2P) shown in orange, with its ion-conducting pore shown in gray. Gray bars indicate the membrane boundaries. b, c – Rat TRPV1 pore structure with α-helical (b) and π-bulge-containing (c) conformation of S6 (PDB ID 7MZD and 7L2P). Only two of four subunits are shown, with the residues lining the pore shown as sticks and labeled. The positions of π-bulge segment, selectivity filter and activation gate are also labeled. Two conformations differ in the structure of activation gate: residues I679 form the narrow constriction when S6 contains the π-bulge, while residues L678 and M682 when S6 is α-helical.
