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

Figure 4.

Figure 4

The grid-like noncovalently interacting mesh network along the PE-dependent minimal gating pathway of the PE-free rTRPV2 channel in an open state at pH8 and 4 °C. (A) The thermoring structure based on cryo-EM data of a single subunit of the open rTRPV2 channel in MNG at pH8 and 4 °C (PDB ID, 6BO4). 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 D344 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 H370-I659 and W660-I524 bridges in the biggest Grid12’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 Grid12ʼ with a 12-residue size to control the H370-I659 and W660-I524 bridges at the pre-S1/TRP/S4–S5 linker interfaces. (C) The structure of the gating Grid2’ with a 2-residue size to control the R459-E358-N673 and W454-W676 bridges at the VSLD/pre-S1/C-terminus interfaces. (D) The sequence of the biggest Grid12ʼ to control the H370-I659 and W660-I524 bridges highlighted in the blue boxes, and the sequence of the gating Grid2ʼ to control the R459-E358-N673 and W454-W676 bridges highlighted in the blue boxes.