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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Phosphatidylinositol 3-phosphate recognition by the FYVE domain.

Recognition of phosphatidylinositol 3-phosphate (Ptdlns(3)P) is crucial for a broad range of cellular signaling and membrane trafficking events regulated by phosphoinositide (PI) 3-kinases. PtdIns(3)P binding by the FYVE domain of human early endosome autoantigen 1 (EEA1), a protein implicated in endosome fusion, involves two beta hairpins and an alpha helix. Specific amino acids, including those of the FYVE domain's conserved RRHHCRQCGNIF motif, contact soluble and micelle-embedded lipid and provide specificity for Ptdlns(3)P over Ptdlns(5)P and Ptdlns, as shown by heteronuclear magnetic resonance spectroscopy. Although the FYVE domain relies on a zinc-binding motif reminiscent of RING fingers, it is distinguished by ovel structural features and its ptdlns(3)P-binding site.[1]


  1. Phosphatidylinositol 3-phosphate recognition by the FYVE domain. Kutateladze, T.G., Ogburn, K.D., Watson, W.T., de Beer, T., Emr, S.D., Burd, C.G., Overduin, M. Mol. Cell (1999) [Pubmed]
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