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

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 ha...

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Detalles Bibliográficos
Autores principales: Ibáñez Shimabukuro, Marina, Rey Burusco, María Florencia, Cooper, A., Kennedy, M. W., Córsico, Betina, Smith, B. O.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2014
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/85218
Aporte de:
id I19-R120-10915-85218
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Bioquímica
Ciencias Médicas
As-p18
Ascaris suum
Fatty acid binding protein
Nematode
nemFABP
Parasite
Biología molecular
spellingShingle Bioquímica
Ciencias Médicas
As-p18
Ascaris suum
Fatty acid binding protein
Nematode
nemFABP
Parasite
Biología molecular
Ibáñez Shimabukuro, Marina
Rey Burusco, María Florencia
Cooper, A.
Kennedy, M. W.
Córsico, Betina
Smith, B. O.
Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
topic_facet Bioquímica
Ciencias Médicas
As-p18
Ascaris suum
Fatty acid binding protein
Nematode
nemFABP
Parasite
Biología molecular
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.
format Articulo
Articulo
author Ibáñez Shimabukuro, Marina
Rey Burusco, María Florencia
Cooper, A.
Kennedy, M. W.
Córsico, Betina
Smith, B. O.
author_facet Ibáñez Shimabukuro, Marina
Rey Burusco, María Florencia
Cooper, A.
Kennedy, M. W.
Córsico, Betina
Smith, B. O.
author_sort Ibáñez Shimabukuro, Marina
title Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum
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
publishDate 2014
url http://sedici.unlp.edu.ar/handle/10915/85218
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