1AZD
CONCANAVALIN FROM CANAVALIA BRASILIENSIS
1AZD の概要
| エントリーDOI | 10.2210/pdb1azd/pdb |
| 分子名称 | CONBR, CALCIUM ION, MANGANESE (II) ION, ... (4 entities in total) |
| 機能のキーワード | legume lectin, lectin |
| 由来する生物種 | Canavalia brasiliensis (Brazilian jackbean) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 102749.78 |
| 構造登録者 | Sanz-Aparicio, J.,Hermoso, J.,Grangeiro, T.B.,Calvete, J.J.,Cavada, B.S. (登録日: 1997-11-16, 公開日: 1998-04-29, 最終更新日: 2024-05-22) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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