3AJ4
Crystal structure of the PH domain of Evectin-2 from human complexed with O-phospho-L-serine
Summary for 3AJ4
| Entry DOI | 10.2210/pdb3aj4/pdb |
| Descriptor | Pleckstrin homology domain-containing family B member 2, PHOSPHOSERINE, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | antiparallel beta sheet, protein transport |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Peripheral membrane protein (Potential): Q96CS7 |
| Total number of polymer chains | 2 |
| Total formula weight | 26565.06 |
| Authors | Okazaki, S.,Kato, R.,Wakatsuki, S. (deposition date: 2010-05-21, release date: 2011-05-25, Last modification date: 2023-11-01) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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