Fig. 5: Identification of PI(4,5)P2 coordination in the hPAC2 channel through structural modeling. | Nature Communications

Fig. 5: Identification of PI(4,5)P2 coordination in the hPAC2 channel through structural modeling.

From: The plasma membrane inner leaflet PI(4,5)P2 is essential for the activation of proton-activated chloride channels

Fig. 5

a Cryo-EM structure models of resting, activated, and desensitized PAC2 channel conformations (Protein Data Bank ID: resting, 7SQG; activated, 7SQF; desensitized, 7SQH). Two black lines indicate the outer and inner plasma membrane surfaces. Blue, red, and green boxes indicate the location of putative PI(4,5)P2-binding residues K333, R335, and K336, respectively. b Molecular docking between K333, R335, and K336 of the activated chain A conformation and PI(4,5)P2 (top) or PI(4)P (bottom). (left) Autodock Vina and UCSF Chimera were used for GIRK PI(4,5)P2 or PI(4)P to the cryo-EM structure of activated PAC2. (right) Nine conformation superpositions of PI(4,5)P2 or PI(4)P. c Docking between K333, R335, and K335 of the desensitized chain A conformation and PI(4,5)P2. (top) Autodock Vina and UCSF Chimera were used for GIRK PI(4,5)P2 to the cryo-EM structure. (bottom) Nine conformation superpositions of PI(4,5)P2. d Hypothetical model of a cytosolic PI(4,5)P2 binding site depending on resting, activated, or desensitized PAC channel conformation.

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