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3M2M

Rat galectin-1 complex with lactose

3M2M の概要
エントリーDOI10.2210/pdb3m2m/pdb
関連するBIRD辞書のPRD_IDPRD_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
Lobsanov, Y.D.,Rini, J.M.,Leffler, H. (登録日: 2010-03-07, 公開日: 2010-07-21, 最終更新日: 2024-11-20)
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: 20873803
DOI: 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)
構造検証レポート
Validation report summary of 3m2m
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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