Extended Data Fig. 8: Comparison of open-state structures of wild-type TRPV3 and Y564A mutant. | Nature Structural & Molecular Biology

Extended Data Fig. 8: Comparison of open-state structures of wild-type TRPV3 and Y564A mutant.

From: Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel

Extended Data Fig. 8

a-b, Overall superposition (RMSD, 2.131 Å) of the open-state structures of wild-type TRPV3 (orange) and previously published Y564A mutant12 (blue, PDB ID: 6PVP) viewed parallel to the membrane (a) and extracellularly (b). c, Single-subunit superposition based on the transmembrane domains (RMSD, 0.943 Å). Note, the most pronounced conformational differences are observed for the S1-S2, S2-S3, S5-P and ARD loops, while the transmembrane domains and TRP helices superpose closely.

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