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

Marc Lenoir; Sara B-M Whittaker; Michael Overduin

doi:10.1007/s12104-011-9296-3

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

Biomol NMR Assign. 2011 Oct;5(2):185-7. doi: 10.1007/s12104-011-9296-3. Epub 2011 Feb 8.

Authors

Marc Lenoir¹, Sara B-M Whittaker, Michael Overduin

Affiliation

¹ Henry Wellcome Building for Biomolecular NMR Spectroscopy, School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.

PMID: 21298564
DOI: 10.1007/s12104-011-9296-3

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adaptor Proteins, Signal Transducing / chemistry*
Adaptor Proteins, Signal Transducing / metabolism
Cholic Acids / chemistry
Golgi Apparatus / chemistry
Humans
Isotopes / chemistry
Micelles
Nuclear Magnetic Resonance, Biomolecular*
Phosphatidylinositol Phosphates / chemistry
Phosphatidylinositol Phosphates / metabolism
Phosphorylcholine / analogs & derivatives
Phosphorylcholine / chemistry
Protein Structure, Secondary
Recombinant Proteins / chemistry

Substances

Adaptor Proteins, Signal Transducing
Cholic Acids
Isotopes
Micelles
PLEKHA3 protein, human
Phosphatidylinositol Phosphates
Recombinant Proteins
phosphatidylinositol 4-phosphate
Phosphorylcholine
dodecylphosphocholine
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

Abstract

Publication types

MeSH terms

Substances

Grants and funding