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2KCJ

solution structure of FAPP1 PH domain

Summary for 2KCJ
Entry DOI10.2210/pdb2kcj/pdb
NMR InformationBMRB: 16082
DescriptorPleckstrin homology domain-containing family A member 3 (1 entity in total)
Functional Keywordsfapp1, ph domain, lipid-binding, membrane, membrane protein
Biological sourceHomo sapiens (Human)
Cellular locationGolgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9HB20
Total number of polymer chains1
Total formula weight12219.89
Authors
Lenoir, M.,Coskun, U.,James, J.,Simons, K.,Overduin, M. (deposition date: 2008-12-22, release date: 2009-12-22, Last modification date: 2024-05-22)
Primary citationLenoir, M.,Coskun, U.,Grzybek, M.,Cao, X.,Buschhorn, S.B.,James, J.,Simons, K.,Overduin, M.
Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains.
Embo Rep., 11:279-284, 2010
Cited by
PubMed Abstract: The mechanisms underlying Golgi targeting and vesiculation are unknown, although the responsible phosphatidylinositol 4-phosphate (PtdIns(4)P) ligand and four-phosphate-adaptor protein (FAPP) modules have been defined. The micelle-bound structure of the FAPP1 pleckstrin homology domain reveals how its prominent wedge independently tubulates Golgi membranes by leaflet penetration. Mutations compromising the exposed hydrophobicity of full-length FAPP2 abolish lipid monolayer binding and compression. The trafficking process begins with an electrostatic approach, phosphoinositide sampling and perpendicular penetration. Extensive protein contacts with PtdIns(4)P and neighbouring phospholipids reshape the bilayer and initiate tubulation through a conserved wedge with features shared by diverse protein modules.
PubMed: 20300118
DOI: 10.1038/embor.2010.28
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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