Fig. 4: Structure of TRPM7 in complex with agonist naltriben.

a Open-state structure TRPM7_NTB-open, with one subunit colored pink and the other three grey and molecules of NTB shown as space-filling models (bright pink). b Pore-forming domain of TRPM7_NTB-Open with the residues contributing to pore lining shown as sticks. Only two of four subunits are shown, with the front and back subunits omitted for clarity. The pore profile is shown as a space-filling model (grey). The π-bulge in the middle of S6 is labeled. c Pore radius for TRPM7-N1098Q_open (yellow), TRPM7_NTB-Open (pink), and TRPM7_Closed (green) calculated using HOLE. The vertical dashed line denotes the radius of a water molecule, 1.4 Å. d Close-up view of the NTB binding site. The molecule of NTB (bright pink) and residues involved in its binding are shown in sticks. e Concentration-dependences for activation of wild-type (WT) and mutant TRPM7 channels by NTB, determined using the Ca²⁺ influx assay as outlined in Supplementary Fig. 7a. Curves through the points (mean ± SEM) are the logistic equation fits; n, the number of independent measurements. The corresponding values of IC₅₀ and n_Hill are provided in Supplementary Table 4. Source data are provided. f Water occupancy of the TRPM7_NTB-Open channel (blue surface) in MD simulations with no applied voltage. The hydroxyl groups of the Y1085 residues that contribute to the permeation pathway are shown as dark blue surfaces. Residues lining the pore are shown in sticks. g Cumulative distribution of K⁺ ions (magenta spheres) in TRPM7_NTB-Open pore during MD simulations under applied voltage.