Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum

Autores
Ibáñez Shimabukuro, Marina; Rey Burusco, María Florencia; Cooper, A.; Kennedy, M. W.; Córsico, Betina; Smith, B. O.
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
As-p18 is produced and secreted by larvae of the parasitic nematode Ascaris suum as they develop within their eggs. The protein is a member of the fatty acid binding protein (FABP) family found in a wide range of eukaryotes, but is distinctive in that it is secreted from the synthesizing cell and has predicted additional structural features not previously seen in other FABPs. As-p18 and similar proteins found only in nematodes have therefore been designated 'nemFABPs'. Sequence-specific 1H, 13C and 15N resonance assignments were established for the 155 amino acid recombinant protein (18.3 kDa) in complex with oleic acid, using a series of three-dimensional triple-resonance heteronuclear NMR experiments. The secondary structure of As-p18 is predicted to be very similar to other FABPs, but the protein has extended loops that have not been observed in other FABPs whose structures have so far been solved.
Facultad de Ciencias Médicas
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Bioquímica
Ciencias Médicas
As-p18
Ascaris suum
Fatty acid binding protein
Nematode
nemFABP
Parasite
Biología molecular
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/85218
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/85218
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suumIbáñez Shimabukuro, MarinaRey Burusco, María FlorenciaCooper, A.Kennedy, M. W.Córsico, BetinaSmith, B. O.BioquímicaCiencias MédicasAs-p18Ascaris suumFatty acid binding proteinNematodenemFABPParasiteBiología molecularAs-p18 is produced and secreted by larvae of the parasitic nematode Ascaris suum as they develop within their eggs. The protein is a member of the fatty acid binding protein (FABP) family found in a wide range of eukaryotes, but is distinctive in that it is secreted from the synthesizing cell and has predicted additional structural features not previously seen in other FABPs. As-p18 and similar proteins found only in nematodes have therefore been designated 'nemFABPs'. Sequence-specific 1H, 13C and 15N resonance assignments were established for the 155 amino acid recombinant protein (18.3 kDa) in complex with oleic acid, using a series of three-dimensional triple-resonance heteronuclear NMR experiments. The secondary structure of As-p18 is predicted to be very similar to other FABPs, but the protein has extended loops that have not been observed in other FABPs whose structures have so far been solved.Facultad de Ciencias MédicasInstituto de Investigaciones Bioquímicas de La Plata2014-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf33-36http://sedici.unlp.edu.ar/handle/10915/85218enginfo:eu-repo/semantics/altIdentifier/issn/1874-2718info:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-012-9447-1info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:24Zoai:sedici.unlp.edu.ar:10915/85218Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:25.13SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
title Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
spellingShingle Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
Ibáñez Shimabukuro, Marina
Bioquímica
Ciencias Médicas
As-p18
Ascaris suum
Fatty acid binding protein
Nematode
nemFABP
Parasite
Biología molecular
title_short Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
title_full Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
title_fullStr Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
title_full_unstemmed Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
title_sort Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
dc.creator.none.fl_str_mv Ibáñez Shimabukuro, Marina
Rey Burusco, María Florencia
Cooper, A.
Kennedy, M. W.
Córsico, Betina
Smith, B. O.
author Ibáñez Shimabukuro, Marina
author_facet Ibáñez Shimabukuro, Marina
Rey Burusco, María Florencia
Cooper, A.
Kennedy, M. W.
Córsico, Betina
Smith, B. O.
author_role author
author2 Rey Burusco, María Florencia
Cooper, A.
Kennedy, M. W.
Córsico, Betina
Smith, B. O.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Bioquímica
Ciencias Médicas
As-p18
Ascaris suum
Fatty acid binding protein
Nematode
nemFABP
Parasite
Biología molecular
topic Bioquímica
Ciencias Médicas
As-p18
Ascaris suum
Fatty acid binding protein
Nematode
nemFABP
Parasite
Biología molecular
dc.description.none.fl_txt_mv As-p18 is produced and secreted by larvae of the parasitic nematode Ascaris suum as they develop within their eggs. The protein is a member of the fatty acid binding protein (FABP) family found in a wide range of eukaryotes, but is distinctive in that it is secreted from the synthesizing cell and has predicted additional structural features not previously seen in other FABPs. As-p18 and similar proteins found only in nematodes have therefore been designated 'nemFABPs'. Sequence-specific 1H, 13C and 15N resonance assignments were established for the 155 amino acid recombinant protein (18.3 kDa) in complex with oleic acid, using a series of three-dimensional triple-resonance heteronuclear NMR experiments. The secondary structure of As-p18 is predicted to be very similar to other FABPs, but the protein has extended loops that have not been observed in other FABPs whose structures have so far been solved.
Facultad de Ciencias Médicas
Instituto de Investigaciones Bioquímicas de La Plata
description As-p18 is produced and secreted by larvae of the parasitic nematode Ascaris suum as they develop within their eggs. The protein is a member of the fatty acid binding protein (FABP) family found in a wide range of eukaryotes, but is distinctive in that it is secreted from the synthesizing cell and has predicted additional structural features not previously seen in other FABPs. As-p18 and similar proteins found only in nematodes have therefore been designated 'nemFABPs'. Sequence-specific 1H, 13C and 15N resonance assignments were established for the 155 amino acid recombinant protein (18.3 kDa) in complex with oleic acid, using a series of three-dimensional triple-resonance heteronuclear NMR experiments. The secondary structure of As-p18 is predicted to be very similar to other FABPs, but the protein has extended loops that have not been observed in other FABPs whose structures have so far been solved.
publishDate 2014
dc.date.none.fl_str_mv 2014-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/85218
url http://sedici.unlp.edu.ar/handle/10915/85218
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1874-2718
info:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-012-9447-1
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
33-36
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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