Figure 9.
Figure 9. PIP2 binding to Kir2 is associated with CD-I rearrangements. (A) Kir6.2 homology model with the location of CD-I residues that cause inactivation when mutated, whether identified in HI patients (red) or experimentally introduced (orange), indicated by spheres centered on the Cα position. (B) In the presence of PIP2 (3SPI), the CD is ∼6 Å closer to the membrane than in the apo cKir2.2 (3JYC) crystal structure. (C) Translocation of CD-I salt bridge residue Cα (ΔCα) in 3JYC relative to 3SPI (structures aligned at R204). Only the R204–E241 salt bridge (3 Å) is preserved in 3JYC. The E241/R325 and D205/R235 intersubunit sidechain distances in 3JYC are beyond those necessary to form salt bridge contacts (residue numbering according to Kir2.1 sequence).

PIP2 binding to Kir2 is associated with CD-I rearrangements. (A) Kir6.2 homology model with the location of CD-I residues that cause inactivation when mutated, whether identified in HI patients (red) or experimentally introduced (orange), indicated by spheres centered on the Cα position. (B) In the presence of PIP2 (3SPI), the CD is ∼6 Å closer to the membrane than in the apo cKir2.2 (3JYC) crystal structure. (C) Translocation of CD-I salt bridge residue Cα (ΔCα) in 3JYC relative to 3SPI (structures aligned at R204). Only the R204–E241 salt bridge (3 Å) is preserved in 3JYC. The E241/R325 and D205/R235 intersubunit sidechain distances in 3JYC are beyond those necessary to form salt bridge contacts (residue numbering according to Kir2.1 sequence).

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