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''' | ==Diversity in the structures and ligand binding sites among the fatty acid and retinol binding proteins of nematodes revealed by Na-FAR-1 from Necator americanus== | ||
<StructureSection load='4uet' size='340' side='right' caption='[[4uet]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uet]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UET FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uet OCA], [http://pdbe.org/4uet PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uet RCSB], [http://www.ebi.ac.uk/pdbsum/4uet PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fatty acid and retinol-binding proteins (FARs) comprise a family of unusual alpha-helix rich lipid-binding proteins found exclusively in nematodes. They are secreted into host tissues by parasites of plants, animals and humans. The structure of a FAR protein from the free-living nematode Caenorhabditis elegans is available, but this protein [C. elegans FAR-7 (Ce-FAR-7)] is from a subfamily of FARs that does not appear to be important at the host/parasite interface. We have therefore examined [Necator americanus FAR-1 (Na-FAR-1)] from the blood-feeding intestinal parasite of humans, N. americanus. The 3D structure of Na-FAR-1 in its ligand-free and ligand-bound forms, determined by NMR (nuclear magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals an alpha-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more complex internal ligand-binding cavity and an additional C-terminal alpha-helix. Titration of apo-Na-FAR-1 with oleic acid, analysed by NMR chemical shift perturbation, reveals that at least four distinct protein-ligand complexes can be formed. Na-FAR-1 and possibly other FARs may have a wider repertoire for hydrophobic ligand binding, as confirmed in the present study by our finding that a range of neutral and polar lipids co-purify with the bacterially expressed recombinant protein. Finally, we show by immunohistochemistry that Na-FAR-1 is present in adult worms with a tissue distribution indicative of possible roles in nutrient acquisition by the parasite and in reproduction in the male. | |||
Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus.,Rey-Burusco MF, Ibanez-Shimabukuro M, Gabrielsen M, Franchini GR, Roe AJ, Griffiths K, Zhan B, Cooper A, Kennedy MW, Corsico B, Smith BO Biochem J. 2015 Nov 1;471(3):403-14. doi: 10.1042/BJ20150068. Epub 2015 Aug 28. PMID:26318523<ref>PMID:26318523</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4uet" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cooper, A]] | |||
[[Category: Corsico, B]] | [[Category: Corsico, B]] | ||
[[Category: Griffiths, K]] | [[Category: Griffiths, K]] | ||
[[Category: Kennedy, M W]] | |||
[[Category: Rey-Burusco, M F]] | |||
[[Category: Shimabukuro, M Ibanez]] | |||
[[Category: Smith, B O]] | |||
[[Category: All-alpha]] | |||
[[Category: Fatty acid binding]] | |||
[[Category: Retinol binding]] | |||
[[Category: Retinol-binding protein]] | |||
Revision as of 22:48, 30 November 2015
Diversity in the structures and ligand binding sites among the fatty acid and retinol binding proteins of nematodes revealed by Na-FAR-1 from Necator americanusDiversity in the structures and ligand binding sites among the fatty acid and retinol binding proteins of nematodes revealed by Na-FAR-1 from Necator americanus
Structural highlights
Publication Abstract from PubMedFatty acid and retinol-binding proteins (FARs) comprise a family of unusual alpha-helix rich lipid-binding proteins found exclusively in nematodes. They are secreted into host tissues by parasites of plants, animals and humans. The structure of a FAR protein from the free-living nematode Caenorhabditis elegans is available, but this protein [C. elegans FAR-7 (Ce-FAR-7)] is from a subfamily of FARs that does not appear to be important at the host/parasite interface. We have therefore examined [Necator americanus FAR-1 (Na-FAR-1)] from the blood-feeding intestinal parasite of humans, N. americanus. The 3D structure of Na-FAR-1 in its ligand-free and ligand-bound forms, determined by NMR (nuclear magnetic resonance) spectroscopy and X-ray crystallography respectively, reveals an alpha-helical fold similar to Ce-FAR-7, but Na-FAR-1 possesses a larger and more complex internal ligand-binding cavity and an additional C-terminal alpha-helix. Titration of apo-Na-FAR-1 with oleic acid, analysed by NMR chemical shift perturbation, reveals that at least four distinct protein-ligand complexes can be formed. Na-FAR-1 and possibly other FARs may have a wider repertoire for hydrophobic ligand binding, as confirmed in the present study by our finding that a range of neutral and polar lipids co-purify with the bacterially expressed recombinant protein. Finally, we show by immunohistochemistry that Na-FAR-1 is present in adult worms with a tissue distribution indicative of possible roles in nutrient acquisition by the parasite and in reproduction in the male. Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus.,Rey-Burusco MF, Ibanez-Shimabukuro M, Gabrielsen M, Franchini GR, Roe AJ, Griffiths K, Zhan B, Cooper A, Kennedy MW, Corsico B, Smith BO Biochem J. 2015 Nov 1;471(3):403-14. doi: 10.1042/BJ20150068. Epub 2015 Aug 28. PMID:26318523[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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