Journal article
Identification of a novel tetrameric structure for human apolipoprotein-D
CS Kielkopf, JKK Low, YF Mok, S Bhatia, T Palasovski, AJ Oakley, AE Whitten, B Garner, SHJ Brown
Journal of Structural Biology | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2018
Abstract
Apolipoprotein-D is a 25 kDa glycosylated member of the lipocalin family that folds into an eight-stranded β-barrel with a single adjacent α-helix. Apolipoprotein-D specifically binds a range of small hydrophobic ligands such as progesterone and arachidonic acid and has an antioxidant function that is in part due to the reduction of peroxidised lipids by methionine-93. Therefore, apolipoprotein-D plays multiple roles throughout the body and is protective in Alzheimer's disease, where apolipoprotein-D overexpression reduces the amyloid-β burden in Alzheimer's disease mouse models. Oligomerisation is a common feature of lipocalins that can influence ligand binding. The native structure of apol..
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Awarded by National Health and Medical Research Council
Funding Acknowledgements
The SAXS experiment was undertaken on the SAXS/WAXS beamline at the Australian Synchrotron, part of ANSTO. The AUC experiments were undertaken at the Macromolecular Interactions Facility, Bio21 Institute, University of Melbourne. Thanks to Kerry-Ann Rye for advice with protein crosslinking, to Timothy Ryan from the SAXS/WAXS beamline at the Australian Synchrotron, part of ANSTO, for help and advice with the SAXS experiments and analysis and to Ann Turnley for proof-reading. BG holds a fellowship from the NHMRC (FT110100249). Travel support for the SAXS experiments was granted by the Australian Synchrotron, part of ANSTO.