Secondary structure and 1H, 13C, 15N resonance assignments of the Golgi-specific PH domain of FAPP1

被引：0
作者：
Marc Lenoir
Sara B.-M. Whittaker
Michael Overduin
机构：
[1] University of Birmingham,Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences
来源：
Biomolecular NMR Assignments | 2011年 / 5卷
关键词：
FAPP1; Pleckstrin homology; PH domain; Phosphoinositide recognition; Phosphatidylinositol 4-phosphate; Trans Golgi network; NMR; Backbone resonance assignment; Secondary structure;
D O I：
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学科分类号：
摘要：
The pleckstrin homology domain of the FAPP1 protein (FAPP1-PH) recognizes phosphatidylinositol 4-phosphate [PtdIns(4)P] and is recruited to the Golgi apparatus in order to mediate trafficking to the cell surface. We report the complete 1H, 13C and 15N resonance assignments of the FAPP1-PH in its free state and those induced by PtdIns(4)P or detergent micelles.
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页码：185 / 187
页数：2
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