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- W2021303199 abstract "Phosphatidylinositol 3-phosphate regulates membrane trafficking and signaling pathways by interacting with the FYVE domains of target proteins. The 1.15 Å structure of the Vps27p FYVE domain reveals two antiparallel β sheets and an α helix stabilized by two Zn2+-binding clusters. The core secondary structures are similar to a rabphilin-3A Zn2+-binding domain and to the C1 and LIM domains. Phosphatidylinositol 3-phosphate binds to a pocket formed by the (R/K)(R/K)HHCR motif. A lattice contact shows how anionic ligands can interact with the phosphatidylinositol 3-phosphate-binding site. The tip of the FYVE domain has basic and hydrophobic surfaces positioned so that nonspecific interactions with the phospholipid bilayer can abet specific binding to phosphatidylinositol 3-phosphate." @default.
- W2021303199 created "2016-06-24" @default.
- W2021303199 creator A5001496532 @default.
- W2021303199 creator A5061450716 @default.
- W2021303199 date "1999-05-01" @default.
- W2021303199 modified "2023-10-02" @default.
- W2021303199 title "Crystal Structure of a Phosphatidylinositol 3-Phosphate-Specific Membrane-Targeting Motif, the FYVE Domain of Vps27p" @default.
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- W2021303199 doi "https://doi.org/10.1016/s0092-8674(00)80776-x" @default.
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