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Solving the FYVE domain–PtdIns(3)P puzzle

Nature Structural Biology volume 8, pages 287–290 (2001)Cite this article

Recent crystallographic analyses of membrane-tethering FYVE finger domains from proteins involved in the regulation of endocytic vesicle trafficking have led to conflicting views of the precise nature of the contacts formed with the specific phospholipid ligand. New NMR data obtained for ligand-bound forms of a FYVE domain help resolve the atomic details of this interaction.

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Figure 1: The chemical structure of PtdIns(3)P and the predicted 'side-on' interaction with the FYVE domain of Vps27p (ref. 10; PDB code 1VFY).
Figure 2: The FYVE homodimer found in the crystal structure of the Drosophila Hrs VHS-FYVE tandem module pair12 (PDB code 1DVP), viewed from the putative ligand binding face (left).
Figure 3: The solution structure of the EEA1 FYVE domain obtained by Kutateladze and Overduin1 coordinates kindly provided by the authors prior to publication) with the headgroup of PtdIns(3)P (magenta) bound to the conserved ligand binding residues (yellow), as obtained from NMR data with soluble di-C4-PtdIns(3)P.

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  1. Department of Biochemistry and Molecular Biology, University College London, Gower Street, London, WC1E 6BT, UK

    Paul C. Driscoll

  2. Ludwig Institute for Cancer Research, 91 Riding House Street, London, W1W 7BS, UK

    Paul C. Driscoll

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Driscoll, P. Solving the FYVE domain–PtdIns(3)P puzzle. Nat Struct Mol Biol 8, 287–290 (2001). https://doi.org/10.1038/86144

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