1AZD
CONCANAVALIN FROM CANAVALIA BRASILIENSIS
Summary for 1AZD
| Entry DOI | 10.2210/pdb1azd/pdb |
| Descriptor | CONBR, CALCIUM ION, MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | legume lectin, lectin |
| Biological source | Canavalia brasiliensis (Brazilian jackbean) |
| Total number of polymer chains | 4 |
| Total formula weight | 102749.78 |
| Authors | Sanz-Aparicio, J.,Hermoso, J.,Grangeiro, T.B.,Calvete, J.J.,Cavada, B.S. (deposition date: 1997-11-16, release date: 1998-04-29, Last modification date: 2024-05-22) |
| Primary citation | Sanz-Aparicio, J.,Hermoso, J.,Grangeiro, T.B.,Calvete, J.J.,Cavada, B.S. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett., 405:114-118, 1997 Cited by PubMed Abstract: Canavalia brasiliensis lectin was isolated from the seeds of a Brazilian autochthonous Leguminosae plant. Despite extensive amino acid sequence similarity with Concanavalin A, C. brasiliensis lectin exerts in vitro and in vivo cellular effects that are markedly different from those displayed by Concanavalin A. We have solved the crystal structure of the C. brasiliensis lectin at 3.0 A resolution. The three-dimensional structure of the lectin monomer can be superimposed onto that of Concanavalin A with a root-mean-square deviation for all C alpha atoms of 0.65 A. However, this parameter is 0.84 and 1.62 A when the C. brasiliensis lectin dimer and tetramer, respectively, are compared with the same structures of Concanavalin A. We suggest that these differences in quaternary structure may account for the different biological properties of these two highly related Leguminosae lectins. PubMed: 9094437DOI: 10.1016/S0014-5793(97)00137-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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