Fig. 3: Structure of hTRPV6Mg in comparison to hTRPV6Open. | Nature Communications

Fig. 3: Structure of hTRPV6Mg in comparison to hTRPV6Open.

From: The locking mechanism of human TRPV6 inhibition by intracellular magnesium

Fig. 3: Structure of hTRPV6Mg in comparison to hTRPV6Open.

a, c Structures of hTRPV6Mg (a) and hTRPV6Open (7S8B) (c) viewed parallel to the membrane (left) and intracellularly (right), with TRPV6 subunits colored yellow, green, pink, and blue. Mg2+ ions in the selectivity filter and at the intracellular pore entry are shown as black and red spheres, respectively. Boxed regions are expanded in (b) and (d). b, d Close-up views of the regions boxed in (a) and (c), with residues contributing to Mg2+ binding shown as sticks. The red arrow in (d) shows rotation of S6 by ~100° that takes D580 away from the Mg2+ binding site.

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