Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3AJ4

Crystal structure of the PH domain of Evectin-2 from human complexed with O-phospho-L-serine

Summary for 3AJ4
Entry DOI10.2210/pdb3aj4/pdb
DescriptorPleckstrin homology domain-containing family B member 2, PHOSPHOSERINE, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsantiparallel beta sheet, protein transport
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Peripheral membrane protein (Potential): Q96CS7
Total number of polymer chains2
Total formula weight26565.06
Authors
Okazaki, S.,Kato, R.,Wakatsuki, S. (deposition date: 2010-05-21, release date: 2011-05-25, Last modification date: 2023-11-01)
Primary citationUchida, 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: 21911378
DOI: 10.1073/pnas.1109101108
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1 Å)
Structure validation

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon