2KCJ

solution structure of FAPP1 PH domain

2KCJ の概要

• エントリーDOI: 10.2210/pdb2kcj/pdb
• NMR情報: BMRB: 16082
• 分子名称: Pleckstrin homology domain-containing family A member 3 (1 entity in total)
• 機能のキーワード: fapp1, ph domain, lipid-binding, membrane, membrane protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9HB20
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12219.89

構造登録者

Lenoir, M.,Coskun, U.,James, J.,Simons, K.,Overduin, M. (登録日: 2008-12-22, 公開日: 2009-12-22, 最終更新日: 2024-05-22)

主引用文献

Lenoir, 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

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

実験手法

SOLUTION NMR