3AJ4
Crystal structure of the PH domain of Evectin-2 from human complexed with O-phospho-L-serine
3AJ4 の概要
| エントリーDOI | 10.2210/pdb3aj4/pdb |
| 分子名称 | Pleckstrin homology domain-containing family B member 2, PHOSPHOSERINE, 1,2-ETHANEDIOL, ... (4 entities in total) |
| 機能のキーワード | antiparallel beta sheet, protein transport |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Membrane; Peripheral membrane protein (Potential): Q96CS7 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 26565.06 |
| 構造登録者 | |
| 主引用文献 | Uchida, Y.,Hasegawa, J.,Chinnapen, D.,Inoue, T.,Okazaki, S.,Kato, R.,Wakatsuki, S.,Misaki, R.,Koike, M.,Uchiyama, Y.,Iemura, S.,Natsume, T.,Kuwahara, R.,Nakagawa, T.,Nishikawa, K.,Mukai, K.,Miyoshi, E.,Taniguchi, N.,Sheff, D.,Lencer, W.I.,Taguchi, T.,Arai, H. Intracellular phosphatidylserine is essential for retrograde membrane traffic through endosomes Proc.Natl.Acad.Sci.USA, 108:15846-15851, 2011 Cited by PubMed Abstract: Phosphatidylserine (PS) is a relatively minor constituent of biological membranes. Despite its low abundance, PS in the plasma membrane (PM) plays key roles in various phenomena such as the coagulation cascade, clearance of apoptotic cells, and recruitment of signaling molecules. PS also localizes in endocytic organelles, but how this relates to its cellular functions remains unknown. Here we report that PS is essential for retrograde membrane traffic at recycling endosomes (REs). PS was most concentrated in REs among intracellular organelles, and evectin-2 (evt-2), a protein of previously unknown function, was targeted to REs by the binding of its pleckstrin homology (PH) domain to PS. X-ray analysis supported the specificity of the binding of PS to the PH domain. Depletion of evt-2 or masking of intracellular PS suppressed membrane traffic from REs to the Golgi. These findings uncover the molecular basis that controls the RE-to-Golgi transport and identify a unique PH domain that specifically recognizes PS but not polyphosphoinositides. PubMed: 21911378DOI: 10.1073/pnas.1109101108 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1 Å) |
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