Show simple item record

dc.contributor.authorSolovyova, Alexandra S.en
dc.contributor.authorMeenan, Nicolaen
dc.contributor.authorMcDermott, Lindsay C.en
dc.contributor.authorGarofalo, Antonioen
dc.contributor.authorBradley, Jannette E.en
dc.contributor.authorKennedy, Malcolm W.en
dc.contributor.authorByron, Olwynen
dc.date.accessioned2018-04-27T10:07:32Z
dc.date.available2018-04-27T10:07:32Z
dc.date.issued2003-08-31
dc.identifier.citationSolovyova AS, Meenan N, McDermott L, Garofalo A, Bradley JE, Kennedy MW, Byron O (2003) 'The polyprotein and FAR lipid binding proteins of nematodes: shape and monomer/dimer states in ligand-free and bound forms', European Biophysics Journal, 32 (5), pp.465-476.en
dc.identifier.issn0175-7571
dc.identifier.pmid12692694
dc.identifier.doi10.1007/s00249-003-0297-8
dc.identifier.urihttp://hdl.handle.net/10547/622677
dc.description.abstractNematodes 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 (approximately 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 v 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 RXRalpha, 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.
dc.language.isoenen
dc.publisherSpringeren
dc.relation.urlhttps://link.springer.com/article/10.1007/s00249-003-0297-8en
dc.rightsGreen - can archive pre-print and post-print or publisher's version/PDF
dc.subjectn-3 polyunsaturated fatty acidsen
dc.subjectC700 Molecular Biology, Biophysics and Biochemistryen
dc.titleThe polyprotein and FAR lipid binding proteins of nematodes: shape and monomer/dimer states in ligand-free and bound formsen
dc.typeArticleen
dc.contributor.departmentUniversity of Glasgowen
dc.contributor.departmentNational Academy of Science of the Ukraineen
dc.contributor.departmentUniversity of Nottinghamen
dc.identifier.journalEuropean Biophysics Journalen
dc.date.updated2018-04-27T09:56:36Z
html.description.abstractNematodes 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 (approximately 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 v 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 RXRalpha, 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.


This item appears in the following Collection(s)

Show simple item record