Journal
NATURE STRUCTURAL BIOLOGY
Volume 8, Issue 4, Pages 287-290Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/86144
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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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