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

Marc Lenoir; SB Whittaker; Michael Overduin

doi:10.1007/s12104-011-9296-3

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

Marc Lenoir, SB Whittaker, Michael Overduin

Research output: Contribution to journal › Article

Abstract

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.

Original language	English
Journal	Biomolecular NMR Assignments
DOIs	https://doi.org/10.1007/s12104-011-9296-3
Publication status	Published - 8 Feb 2011

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10.1007/s12104-011-9296-3

NMR Studies of Membrane Associated Proteins
Overduin, M.
Biotechnology & Biological Sciences Research Council
1/10/04 → 30/09/07
Project: Research Councils

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title = "Secondary structure and (1)H, (13)C, (15)N resonance assignments of the Golgi-specific PH domain of FAPP1.",

abstract = "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.",

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AU - Whittaker, SB

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N2 - 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.

AB - 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.

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DO - 10.1007/s12104-011-9296-3

M3 - Article

C2 - 21298564

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

ER -

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

Abstract

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NMR Studies of Membrane Associated Proteins

Cite this