INVESTIGADORES
IRAZOQUI Fernando Jose
artículos
Título:
Crystallization and preliminary X-ray study of the common edible mushroom (Agaricus bisporus) lectin.
Autor/es:
CARRIZO ME,; FERNANDO JOSE IRAZOQUI; LARDONE RD,; NORES GA,; CURTINO JA,; CAPALDI S,; PERDUCA M,; MONACO HL,
Revista:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Referencias:
Año: 2004 vol. 60 p. 718 - 720
ISSN:
0907-4449
Resumen:
Crystallization and preliminary X-ray study of the common edible mushroom ( Agaricus bisporus) lectin
Maria E. Carrizo, Fernando J. Irazoqui, Ricardo D. Lardone, Gustavo A. Nores, Juan A. Curtino, Stefano Capaldi, Massimiliano Perduca and Hugo L. Monaco
Acta Crystallographica Section D
Biological
Crystallography
(2004). D60, 718720
ISSN 0907-4449
Editors: E. N. Baker and Z. Dauter
The lectin from the common edible mushroom Agaricus bisporus
(ABL) belongs to the group of proteins that have the property of
binding the Thomsen±Friedenreich antigen (T-antigen) selectively
and with high afÆnity, but does not show any sequence similarity to
the other proteins that share this property. The ABL sequence is
instead similar to those of members of the saline-soluble fungal
lectins, a protein family with pesticidal properties. The presence of
different isoforms has been reported. It has been found that in order
to be able to grow diffraction-quality crystals of the lectin, it is
essential to separate the isoforms, which was performed by
preparative isoelectric focusing. Using standard procedures, it was
possible to crystallize the most basic of the forms by either vapour
diffusion or equilibrium dialysis, but attempts to grow crystals of the
other more acidic forms were unsuccessful. The ABL crystals belong
to the orthorhombic space group C2221, with unit-cell parameters
a = 93.06, b = 98.16, c = 76.38 A , and diffract to a resolution of 2.2 A
on a conventional source at room temperature. It is expected that the
solution of this structure will yield further valuable information on
the differences in the T-antigen-binding folds and will perhaps help to
clarify the details of the ligand binding to the protein.