3M2M
Rat galectin-1 complex with lactose
3M2M の概要
| エントリーDOI | 10.2210/pdb3m2m/pdb |
| 関連するBIRD辞書のPRD_ID | PRD_900004 |
| 分子名称 | Galectin-1, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (2 entities in total) |
| 機能のキーワード | galectin-1, lectin, beta sandwich, extracellular matrix, secreted, carbohydrate-binding protein |
| 由来する生物種 | Rattus norvegicus (brown rat,rat,rats) |
| 細胞内の位置 | Secreted, extracellular space, extracellular matrix (By similarity): P11762 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 119900.49 |
| 構造登録者 | |
| 主引用文献 | Salomonsson, E.,Larumbe, A.,Tejler, J.,Tullberg, E.,Rydberg, H.,Sundin, A.,Khabut, A.,Frejd, T.,Lobsanov, Y.D.,Rini, J.M.,Nilsson, U.J.,Leffler, H. Monovalent interactions of galectin-1. Biochemistry, 49:9518-9532, 2010 Cited by PubMed Abstract: Galectin-1, a β-galactoside binding lectin involved in immunoregulation and cancer, binds natural and many synthetic multivalent glycoconjugates with an apparent glycoside cluster effect, that is, affinity above and beyond what would be expected from the concentration of the determinant sugar. Here we have analyzed the mechanism of such cluster effects in solution at physiological concentration using a fluorescence anisotropy assay with a novel fluorescent high-affinity galectin-1 binding probe. The interaction of native dimeric and monomeric mutants of rat and human galectin-1 with mono- and divalent small molecules, fetuin, asialofetuin, and human serum glycoproteins was analyzed. Surprisingly, high-affinity binding did not depend much on the dimeric state of galectin-1 and thus is due mainly to monomeric interactions of a single carbohydrate recognition domain. The mechanism for this is unknown, but one possibility includes additional interactions that high-affinity ligands make with an extended binding site on the carbohydrate recognition domain. It follows that such weak additional interactions must be important for the biological function of galectin-1 and also for the design of galectin-1 inhibitors. PubMed: 20873803DOI: 10.1021/bi1009584 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.95 Å) |
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