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- W2904804702 abstract "INAD assembles key enzymes of the Drosophila compound eye photo-transduction pathway into a supramolecular complex, supporting efficient and fast light signaling. However, the molecular mechanism that governs the interaction between INAD and NORPA (phospholipase Cβ, PLCβ), a key step for the fast kinetics of the light signaling, is not known. Here, we show that the NORPA C-terminal coiled-coil domain and PDZ-binding motif (CC-PBM) synergistically bind to INAD PDZ45 tandem with an unexpected mode and unprecedented high affinity. Guided by the structure of the INAD-NORPA complex, we discover that INADL is probably a mammalian counterpart of INAD. The INADL PDZ89 tandem specifically binds to PLCβ4 with a mode that is strikingly similar to that of the INAD-NORPA complex, as revealed by the structure of the INADL PDZ89-PLCβ4 CC-PBM complex. Therefore, our study suggests that the highly specific PDZ tandem - PLCβ interactions are an evolutionarily conserved mechanism in PLCβ signaling in the animal kingdom." @default.
- W2904804702 created "2018-12-22" @default.
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- W2904804702 date "2018-12-10" @default.
- W2904804702 modified "2023-09-24" @default.
- W2904804702 title "An unexpected INAD PDZ tandem-mediated plc beta binding inDrosophilaphoto receptors." @default.
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- W2904804702 doi "https://doi.org/10.2210/pdb6ire/pdb" @default.
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