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[Preprint]. 2025 Feb 21:rs.3.rs-6049325. [Version 1] doi: 10.21203/rs.3.rs-6049325/v1

Figure 5.

Figure 5

The grid-like noncovalently interacting mesh network along the PE-dependent minimal gating pathway of the PE-free rTRPV2 channel in a partially open state at pH8 and 4 °C. (A) The thermoring structure based on cryo-EM data of a single subunit of the partially open rTRPV2 channel in MNG at pH8 and 4 °C (PDB ID, 6BO5). The pore domain, the S4–S5 linker, the TRP domain, and the pre-S1 domain are indicated by black arrows except for the VSLD. Salt bridges, π interactions, and H-bonds between paired amino acid side chains along the PE-dependent minimal gating pathway from D349 to R684 are marked in purple, green, and orange, respectively. The specific grid sizes required to control the least-stable noncovalent interactions in the grids are labeled with black numbers. The F540-L641 and F547-Y629 bridges in the biggest Grid14 are highlighted. The total grid sizes and the total grid size-controlled noncovalent interactions along the PE-dependent minimal gating pathway are shown in cyan and black circles, respectively. (B) The structure of the biggest Grid14 with a 14-residue size to control the F540-L641 and F547-Y629 bridges at the S5/S6 interface. (C) The structure of the potentially thermosensitive Grid12” with a 12-residue size to control the D349-R684 and E358-R459 bridges at the VSLD/pre-S1/C terminus interfaces. (D) The sequence of the biggest Grid14 to control the F540-L641 and F547-Y629 bridges highlighted in the blue boxes. Additionally, sequence alignment of the potentially thermosensitive Grid12” is shown between rTRPV2 and hTRPV2.