Solving the FYVE domain–PtdIns(3)P puzzle

被引：0
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作者：
Paul C. Driscoll
机构：
[1] University College London,Department of Biochemistry and Molecular Biology
[2] Ludwig Institute for Cancer Research,undefined
来源：
Nature Structural Biology | 2001年 / 8卷
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摘要：
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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页码：287 / 290
页数：3
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