THE CRYSTAL-STRUCTURE OF CANAVALIA-BRASILIENSIS LECTIN SUGGESTS A CORRELATION BETWEEN ITS QUATERNARY CONFORMATION AND ITS DISTINCT BIOLOGICAL PROPERTIES FROM CONCANAVALIN-A
J. Sanzaparicio et al., THE CRYSTAL-STRUCTURE OF CANAVALIA-BRASILIENSIS LECTIN SUGGESTS A CORRELATION BETWEEN ITS QUATERNARY CONFORMATION AND ITS DISTINCT BIOLOGICAL PROPERTIES FROM CONCANAVALIN-A, FEBS letters, 405(1), 1997, pp. 114-118
Canavalia brasiliensis lectin was isolated from the seeds of a Brazili
an autochthonous Leguminosae plant. Despite extensive amino acid seque
nce similarity with Concanavalin A, C. brasiliensis lectin exerts in v
itro and in vivo cellular effects that are markedly different from tho
se displayed by Concanavalin A. We have solved the crystal structure o
f the C. brasiliensis lectin at 3.0 Angstrom resolution. The three-dim
ensional structure of the lectin monomer can be superimposed onto that
of Concanavalin A with a root-mean-square deviation for all C alpha a
toms of 0.65 Angstrom. However, this parameter is 0.84 and 1.62 Angstr
om when the C. brasiliensis lectin diner and tetramer, respectively, a
re compared with the same structures of Concanavalin A. We suggest tha
t these differences in quaternary structure may account for the differ
ent biological properties of these two highly related Leguminosae lect
ins. (C) 1997 Federation of European Biochemical Societies.