Linked Life Data

12692694

Source:http://linkedlifedata.com/resource/pubmed/id/12692694

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-8-27
pubmed:abstractText
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 (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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0175-7571
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
465-76
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12692694-Allergens, pubmed-meshheading:12692694-Amino Acid Sequence, pubmed-meshheading:12692694-Animals, pubmed-meshheading:12692694-Ascaris, pubmed-meshheading:12692694-Binding Sites, pubmed-meshheading:12692694-Caenorhabditis elegans, pubmed-meshheading:12692694-Caenorhabditis elegans Proteins, pubmed-meshheading:12692694-Carrier Proteins, pubmed-meshheading:12692694-Centrifugation, Density Gradient, pubmed-meshheading:12692694-Computer Simulation, pubmed-meshheading:12692694-Dimerization, pubmed-meshheading:12692694-Ligands, pubmed-meshheading:12692694-Lipids, pubmed-meshheading:12692694-Macromolecular Substances, pubmed-meshheading:12692694-Models, Molecular, pubmed-meshheading:12692694-Molecular Sequence Data, pubmed-meshheading:12692694-Molecular Weight, pubmed-meshheading:12692694-Onchocerca, pubmed-meshheading:12692694-Particle Size, pubmed-meshheading:12692694-Polyproteins, pubmed-meshheading:12692694-Protein Binding, pubmed-meshheading:12692694-Protein Conformation, pubmed-meshheading:12692694-Recombinant Proteins, pubmed-meshheading:12692694-Sequence Analysis, Protein, pubmed-meshheading:12692694-Sequence Homology, Amino Acid, pubmed-meshheading:12692694-Structure-Activity Relationship, pubmed-meshheading:12692694-X-Ray Diffraction
pubmed:year
2003
pubmed:articleTitle
The polyprotein and FAR lipid binding proteins of nematodes: shape and monomer/dimer states in ligand-free and bound forms.
pubmed:affiliation
Division of Infection and Immunity, Institute of Biomedical and Life Sciences, Joseph Black Building, University of Glasgow, Glasgow, G12 8QQ, UK. alexandra.solovyova@bio.gla.ac.uk
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't, Evaluation Studies