FAPP1的高尔基体特异性PH结构域的二级结构以及1H、13C、15N共振归属
Secondary structure and 1H, 13C, 15N resonance assignments of the Golgi-specific PH domain of FAPP1.
作者信息
Lenoir Marc, Whittaker Sara B-M, Overduin Michael
机构信息
Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
出版信息
Biomol NMR Assign. 2011 Oct;5(2):185-7. doi: 10.1007/s12104-011-9296-3. Epub 2011 Feb 8.
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 (1)H, (13)C and (15)N resonance assignments of the FAPP1-PH in its free state and those induced by PtdIns(4)P or detergent micelles.
FAPP1蛋白的普列克底物蛋白同源结构域（FAPP1-PH）可识别磷脂酰肌醇4-磷酸[PtdIns(4)P]，并被招募至高尔基体以介导向细胞表面的运输。我们报告了处于游离状态以及由PtdIns(4)P或去污剂胶束诱导状态下FAPP1-PH的完整氢-1、碳-13和氮-15共振归属。
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