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| Content Provider | Springer Nature Link |
|---|---|
| Author | Solovyova, Alexandra S. Meenan, Nicola McDermott, Lindsay Garofalo, Antonio Bradley, Jannette E. Kennedy, Malcolm W. Byron, Olwyn |
| Copyright Year | 2003 |
| Abstract | Nematodes produce two classes of small, helix-rich fatty acid- and retinol-binding proteins whose structures and in vivo functions remain to be elucidated. These are the polyprotein allergens (NPA) and the FAR proteins. The solution properties of recombinant forms of these proteins from parasitic [Ascaris suum (As) and Onchocerca volvulus (Ov)] and free-living [Caenorhabditis elegans (Ce)] nematodes have been examined. Analytical ultracentrifugation (AUC) showed that, contrary to previous findings, the rAs-NPA-1A polyprotein unit (~15 kDa) is a monomer, and this stoichiometry is unaltered by ligand (oleic acid) binding. The rOv-FAR-1 and rCe-FAR-5 proteins differ in that the former forms a tight dimer and the latter a monomer, and these oligomeric states are also unaffected by ligand binding or protein concentration. Sedimentation equilibrium experiments showed that the partial specific volume v̄ of the unliganded proteins agree well with the value calculated from amino acid composition extrapolated to experimental temperature, and was unaffected upon ligand binding. Data from small-angle X-ray scattering (SAXS) indicated that both of the monomeric proteins rAs-NPA-1A and rCe-FAR-5 are globular, although slightly elongated and flattened. These data are in good agreement with shapes predicted from sedimentation velocity experiments and hydrodynamic bead modelling. On the basis of functional and secondary structural homology with the ligand-binding domain of the retinoic acid receptor RXRα, de novo atomic resolution structures for rAs-NPA-1A and rCe-FAR-5 have been constructed which are consistent with the SAXS and hydrodynamic data. |
| Starting Page | 465 |
| Ending Page | 476 |
| Page Count | 12 |
| File Format | |
| ISSN | 01757571 |
| Journal | European Biophysics Journal |
| Volume Number | 32 |
| Issue Number | 5 |
| e-ISSN | 14321017 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2003-04-12 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Analytical ultracentrifugation Hydrodynamic bead modelling Nematode fatty acid binding proteins Protein-ligand interaction Small-angle X-ray scattering |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Biophysics |
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