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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDD83 |
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![]() | Apolipoprotein D (ApoD) tetramer
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Function / homology | ![]() negative regulation of lipoprotein lipid oxidation / negative regulation of T cell migration / Transport of fatty acids / negative regulation of smooth muscle cell-matrix adhesion / peripheral nervous system axon regeneration / negative regulation of focal adhesion assembly / tissue regeneration / lipid transporter activity / negative regulation of monocyte chemotactic protein-1 production / negative regulation of platelet-derived growth factor receptor signaling pathway ...negative regulation of lipoprotein lipid oxidation / negative regulation of T cell migration / Transport of fatty acids / negative regulation of smooth muscle cell-matrix adhesion / peripheral nervous system axon regeneration / negative regulation of focal adhesion assembly / tissue regeneration / lipid transporter activity / negative regulation of monocyte chemotactic protein-1 production / negative regulation of platelet-derived growth factor receptor signaling pathway / negative regulation of protein import into nucleus / cholesterol binding / response to axon injury / negative regulation of cytokine production involved in inflammatory response / cytosolic ribosome / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / response to reactive oxygen species / negative regulation of smooth muscle cell proliferation / lipid metabolic process / brain development / glucose metabolic process / angiogenesis / neuronal cell body / dendrite / perinuclear region of cytoplasm / endoplasmic reticulum / extracellular space / extracellular exosome / extracellular region / cytoplasm Similarity search - Function |
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![]() | ![]() Title: Identification of a novel tetrameric structure for human apolipoprotein-D. Authors: Claudia S Kielkopf / Jason K K Low / Yee-Foong Mok / Surabhi Bhatia / Tony Palasovski / Aaron J Oakley / Andrew E Whitten / Brett Garner / Simon H J Brown / ![]() 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 ...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 apolipoprotein-D, however, has not been conclusively defined. Apolipoprotein-D is generally described as a monomeric protein, although it dimerises when reducing peroxidised lipids. Here, we investigated the native structure of apolipoprotein-D derived from plasma, breast cyst fluid (BCF) and cerebrospinal fluid. In plasma and cerebrospinal fluid, apolipoprotein-D was present in high-molecular weight complexes, potentially in association with lipoproteins. In contrast, apolipoprotein-D in BCF formed distinct oligomeric species. We assessed apolipoprotein-D oligomerisation using native apolipoprotein-D purified from BCF and a suite of complementary methods, including multi-angle laser light scattering, analytical ultracentrifugation and small-angle X-ray scattering. Our analyses showed that apolipoprotein-D predominantly forms a ∼95 to ∼100 kDa tetramer. Small-angle X-ray scattering analysis confirmed these findings and provided a structural model for apolipoprotein-D tetramer. These data indicate apolipoprotein-D rarely exists as a free monomer under physiological conditions and provide insights into novel native structures of apolipoprotein-D and into oligomerisation behaviour in the lipocalin family. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
Model #2054 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Symmetry: P222 Comment: The restraints used are 32 Ang between: a)K55-K55; b) K156-K156; c) K155-K156 and; d) K144-K156 Chi-square value: 1.28 ![]() |
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Model #2055 | ![]() Type: atomic / Radius of dummy atoms: 1.90 A / Symmetry: P222 Comment: The restraints used are 32 Ang between: a) K55-K55; b) K156-K156; c) K155-K156 and; d) K144-K156. Chi-square value: 1.26 ![]() |
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Sample
![]() | Name: Apolipoprotein D (ApoD) tetramer |
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Buffer | Name: 50 mM Na Phosphate, 150 mM NaCl, 3% glycerol / pH: 7.4 |
Entity #956 | Name: ApoD / Type: protein / Description: Apolipoprotein D / Formula weight: 19.303 / Num. of mol.: 4 / Source: Homo sapiens / References: UniProt: P05090 Sequence: QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLS |
-Experimental information
Beam | Instrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia ![]() | |||||||||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M / Pixsize x: 172 mm | |||||||||||||||||||||||||||||||||||||||
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Distance distribution function P(R) |
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Result | Comments: Additional SEC-SAXS information: SEC-column: GE Healthcare Superdex S200 5/150; Loading concentration (measured using BCA assay): 7.5 mg/ml; Injection volume : 50 µl; Flow rate: 0.45 ...Comments: Additional SEC-SAXS information: SEC-column: GE Healthcare Superdex S200 5/150; Loading concentration (measured using BCA assay): 7.5 mg/ml; Injection volume : 50 µl; Flow rate: 0.45 ml/min; Number of frames averaged over the elution peak: 15. The starting pdb model was the apo-form of apoD with modelled glycans (Oakley et al. 2012). The refined SASREF CV model incorporated contact restraints derived from crosslinking mass spectrometry (crosslinker BS3) that are included in the full entry zip archive (32 Ang between: a, K55-K55; b, K156-K156; c, K155-K156 and; d, K144-K156.)
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