1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus
- Autores
- Rey Burusco, María Florencia; Ibáñez Shimabukuro, Marina; Cooper, A.; Kennedy, Malcolm W.; Córsico, Betina; Smith, Brian O.
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The fatty acid and retinol-binding (FAR) proteins are a family of unusual helix-rich lipid binding proteins found exclusively in nematodes, and are secreted by a range of parasites of humans, animals and plants. Na-FAR-1 is from the parasitic nematode Necator americanus, an intestinal blood-feeding parasite of humans. Sequence-specific 1H, 13C and 15N resonance assignments have been obtained for the recombinant 170 amino acid protein, using three-dimensional triple-resonance heteronuclear magnetic resonance experiments. Backbone assignments have been obtained for 99.3 % of the non-proline HN/N pairs (146 out of 147). The amide resonance of T45 was not observed, probably due to rapid exchange with solvent water. A total of 96.9 % of backbone resonances were identified, while 97.7 % assignment of amino acid sidechain protons is complete. All Hα(166), Hβ(250) and Hγ(160) and 98.4 % of the Hδ (126 out of 128) atoms were assigned. In addition, 99.4 % Cα (154 out of 155) and 99.3 % Cβ (143 out of 144) resonances have been assigned. No resonances were observed for the NHn groups of R93 NεHε, arginine, Nη1H2, Nη2H2, histidine Nδ1Hδ1, Nε1Hε1 and lysine Nζ3H3. Na-FAR-1 has a similar overall arrangement of α-helices to Ce-FAR-7 of the free-living Caeorhabditis elegans, but with an extra C-terminal helix.
Facultad de Ciencias Médicas
Instituto de Investigaciones Bioquímicas de La Plata - Materia
-
Ciencias Médicas
Fatty-acid and retinol-binding protein
Na-FAR-1
Necator americanus
NMR
Parasitic nematode - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/85270
Ver los metadatos del registro completo
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1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanusRey Burusco, María FlorenciaIbáñez Shimabukuro, MarinaCooper, A.Kennedy, Malcolm W.Córsico, BetinaSmith, Brian O.Ciencias MédicasFatty-acid and retinol-binding proteinNa-FAR-1Necator americanusNMRParasitic nematodeThe fatty acid and retinol-binding (FAR) proteins are a family of unusual helix-rich lipid binding proteins found exclusively in nematodes, and are secreted by a range of parasites of humans, animals and plants. Na-FAR-1 is from the parasitic nematode <i>Necator americanus</i>, an intestinal blood-feeding parasite of humans. Sequence-specific <SUP>1</SUP>H, <SUP>13</SUP>C and <SUP>15</SUP>N resonance assignments have been obtained for the recombinant 170 amino acid protein, using three-dimensional triple-resonance heteronuclear magnetic resonance experiments. Backbone assignments have been obtained for 99.3 % of the non-proline HN/N pairs (146 out of 147). The amide resonance of T45 was not observed, probably due to rapid exchange with solvent water. A total of 96.9 % of backbone resonances were identified, while 97.7 % assignment of amino acid sidechain protons is complete. All Hα(166), Hβ(250) and Hγ(160) and 98.4 % of the Hδ (126 out of 128) atoms were assigned. In addition, 99.4 % Cα (154 out of 155) and 99.3 % Cβ (143 out of 144) resonances have been assigned. No resonances were observed for the NH<SUB>n</SUB> groups of R93 N<SUB>ε</SUB>H<SUB>ε</SUB>, arginine, N<SUB>η1</SUB>H<SUB>2</SUB>, N<SUB>η2</SUB>H<SUB>2</SUB>, histidine N<SUB>δ1</SUB>H<SUB>δ1</SUB>, N<SUB>ε1</SUB>H<SUB>ε1</SUB> and lysine N<SUB>ζ3</SUB>H<SUB>3</SUB>. Na-FAR-1 has a similar overall arrangement of α-helices to Ce-FAR-7 of the free-living <i>Caeorhabditis elegans</i>, but with an extra C-terminal helix.Facultad de Ciencias MédicasInstituto de Investigaciones Bioquímicas de La Plata2014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf19-21http://sedici.unlp.edu.ar/handle/10915/85270enginfo:eu-repo/semantics/altIdentifier/issn/1874-2718info:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-012-9444-4info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:24Zoai:sedici.unlp.edu.ar:10915/85270Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:25.133SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus |
title |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus |
spellingShingle |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus Rey Burusco, María Florencia Ciencias Médicas Fatty-acid and retinol-binding protein Na-FAR-1 Necator americanus NMR Parasitic nematode |
title_short |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus |
title_full |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus |
title_fullStr |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus |
title_full_unstemmed |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus |
title_sort |
1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus |
dc.creator.none.fl_str_mv |
Rey Burusco, María Florencia Ibáñez Shimabukuro, Marina Cooper, A. Kennedy, Malcolm W. Córsico, Betina Smith, Brian O. |
author |
Rey Burusco, María Florencia |
author_facet |
Rey Burusco, María Florencia Ibáñez Shimabukuro, Marina Cooper, A. Kennedy, Malcolm W. Córsico, Betina Smith, Brian O. |
author_role |
author |
author2 |
Ibáñez Shimabukuro, Marina Cooper, A. Kennedy, Malcolm W. Córsico, Betina Smith, Brian O. |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Ciencias Médicas Fatty-acid and retinol-binding protein Na-FAR-1 Necator americanus NMR Parasitic nematode |
topic |
Ciencias Médicas Fatty-acid and retinol-binding protein Na-FAR-1 Necator americanus NMR Parasitic nematode |
dc.description.none.fl_txt_mv |
The fatty acid and retinol-binding (FAR) proteins are a family of unusual helix-rich lipid binding proteins found exclusively in nematodes, and are secreted by a range of parasites of humans, animals and plants. Na-FAR-1 is from the parasitic nematode <i>Necator americanus</i>, an intestinal blood-feeding parasite of humans. Sequence-specific <SUP>1</SUP>H, <SUP>13</SUP>C and <SUP>15</SUP>N resonance assignments have been obtained for the recombinant 170 amino acid protein, using three-dimensional triple-resonance heteronuclear magnetic resonance experiments. Backbone assignments have been obtained for 99.3 % of the non-proline HN/N pairs (146 out of 147). The amide resonance of T45 was not observed, probably due to rapid exchange with solvent water. A total of 96.9 % of backbone resonances were identified, while 97.7 % assignment of amino acid sidechain protons is complete. All Hα(166), Hβ(250) and Hγ(160) and 98.4 % of the Hδ (126 out of 128) atoms were assigned. In addition, 99.4 % Cα (154 out of 155) and 99.3 % Cβ (143 out of 144) resonances have been assigned. No resonances were observed for the NH<SUB>n</SUB> groups of R93 N<SUB>ε</SUB>H<SUB>ε</SUB>, arginine, N<SUB>η1</SUB>H<SUB>2</SUB>, N<SUB>η2</SUB>H<SUB>2</SUB>, histidine N<SUB>δ1</SUB>H<SUB>δ1</SUB>, N<SUB>ε1</SUB>H<SUB>ε1</SUB> and lysine N<SUB>ζ3</SUB>H<SUB>3</SUB>. Na-FAR-1 has a similar overall arrangement of α-helices to Ce-FAR-7 of the free-living <i>Caeorhabditis elegans</i>, but with an extra C-terminal helix. Facultad de Ciencias Médicas Instituto de Investigaciones Bioquímicas de La Plata |
description |
The fatty acid and retinol-binding (FAR) proteins are a family of unusual helix-rich lipid binding proteins found exclusively in nematodes, and are secreted by a range of parasites of humans, animals and plants. Na-FAR-1 is from the parasitic nematode <i>Necator americanus</i>, an intestinal blood-feeding parasite of humans. Sequence-specific <SUP>1</SUP>H, <SUP>13</SUP>C and <SUP>15</SUP>N resonance assignments have been obtained for the recombinant 170 amino acid protein, using three-dimensional triple-resonance heteronuclear magnetic resonance experiments. Backbone assignments have been obtained for 99.3 % of the non-proline HN/N pairs (146 out of 147). The amide resonance of T45 was not observed, probably due to rapid exchange with solvent water. A total of 96.9 % of backbone resonances were identified, while 97.7 % assignment of amino acid sidechain protons is complete. All Hα(166), Hβ(250) and Hγ(160) and 98.4 % of the Hδ (126 out of 128) atoms were assigned. In addition, 99.4 % Cα (154 out of 155) and 99.3 % Cβ (143 out of 144) resonances have been assigned. No resonances were observed for the NH<SUB>n</SUB> groups of R93 N<SUB>ε</SUB>H<SUB>ε</SUB>, arginine, N<SUB>η1</SUB>H<SUB>2</SUB>, N<SUB>η2</SUB>H<SUB>2</SUB>, histidine N<SUB>δ1</SUB>H<SUB>δ1</SUB>, N<SUB>ε1</SUB>H<SUB>ε1</SUB> and lysine N<SUB>ζ3</SUB>H<SUB>3</SUB>. Na-FAR-1 has a similar overall arrangement of α-helices to Ce-FAR-7 of the free-living <i>Caeorhabditis elegans</i>, but with an extra C-terminal helix. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014 |
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eng |
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eng |
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