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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/85270
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/85270
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling 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:UNLP2025-10-22T16:57:12Zoai: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:13292025-10-22 16:57:13.053SEDICI (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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info:eu-repo/semantics/publishedVersion
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dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/85270
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language eng
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info:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-012-9444-4
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
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