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dc.contributor.author
Curto, Lucrecia María
dc.contributor.author
Caramelo, Julio Javier
dc.contributor.author
Delfino, Jose Maria
dc.date.available
2018-03-19T19:41:39Z
dc.date.issued
2005-10
dc.identifier.citation
Curto, Lucrecia María; Caramelo, Julio Javier; Delfino, Jose Maria; Δ98Δ, a functional all-β-sheet abridged form of intestinal fatty acid binding protein; American Chemical Society; Biochemistry; 44; 42; 10-2005; 13847-13857
dc.identifier.issn
0006-2960
dc.identifier.uri
http://hdl.handle.net/11336/39256
dc.description.abstract
Intestinal fatty acid binding protein (IFABP) is a 15 kDa intracellular lipid-binding protein exhibiting a ́-barrel fold that resembles a clamshell. The ́-barrel, which encloses the ligand binding cavity, consists of two perpendicular five-stranded ́-sheets with an intervening helix-turn-helix motif between strands A and B. Δ98Δ (fragment 29-126 of IFABP) was obtained either in its recombinant form or by limited proteolysis with clostripain. Despite lacking extensive stretches involved in the closure of the β-barrel, Δ98Δ remains soluble and stable in solution. Spectroscopic analyses by circular dichroism, ultraviolet absorption, and intrinsic fluorescence indicate that the fragment retains substantial β-sheet content and tertiary interactions. In particular, the environment around W82 is identical in both Δ98Δ and IFABP, a fact consistent with the conservation in the former of all the critical amino acid residues belonging to the hydrophobic core. In addition, the Stokes radius of Δ98Δ is similar to that of IFABP and 16% larger than that calculated from its molecular weight (11 kDa). The monomeric status of Δ98Δ was further confirmed by chemical cross-linking experiments. Although lacking 25% of the amino acids of the parent protein, in the presence of GdnHCl, Δ98Δ unfolds through a cooperative transition showing a midpoint at 0.90 M. Remarkably, it also preserves binding activity for fatty acids (K d = 5.1 μM for oleic acid and Kd = 0.72 μM for trans-parinaric acid), a fact that exerts a stabilizing effect on its structure. These cumulative evidences show that Δ98Δ adopts a monomeric state with a compact core and a loose periphery, being so far the smallest structure of its kind preserving binding function.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Ifabp
dc.subject
Abridged Variant
dc.subject
Truncation
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Δ98Δ, a functional all-β-sheet abridged form of intestinal fatty acid binding protein
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-15T18:03:28Z
dc.identifier.eissn
1520-4995
dc.journal.volume
44
dc.journal.number
42
dc.journal.pagination
13847-13857
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
Fil: Curto, Lucrecia María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil
Fil: Caramelo, Julio Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.journal.title
Biochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bi051080s
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/bi051080s
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