1A3K
X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION
1A3K の概要
エントリーDOI | 10.2210/pdb1a3k/pdb |
分子名称 | GALECTIN-3, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
機能のキーワード | galectin, galaptin, lectin, ige-binding protein |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 15987.28 |
構造登録者 | Seetharaman, J.,Kanigsberg, A.,Slaaby, R.,Leffler, H.,Barondes, S.H.,Rini, J.M. (登録日: 1998-01-22, 公開日: 1998-07-15, 最終更新日: 2024-02-07) |
主引用文献 | Seetharaman, J.,Kanigsberg, A.,Slaaby, R.,Leffler, H.,Barondes, S.H.,Rini, J.M. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution. J.Biol.Chem., 273:13047-13052, 1998 Cited by PubMed Abstract: Galectins are a family of lectins which share similar carbohydrate recognition domains (CRDs) and affinity for small beta-galactosides, but which show significant differences in binding specificity for more complex glycoconjugates. We report here the x-ray crystal structure of the human galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A resolution. This structure represents the first example of a CRD determined from a galectin which does not show the canonical 2-fold symmetric dimer organization. Comparison with the published structures of galectins-1 and -2 provides an explanation for the differences in carbohydrate-binding specificity shown by galectin-3, and for the fact that it fails to form dimers by analogous CRD-CRD interactions. PubMed: 9582341DOI: 10.1074/jbc.273.21.13047 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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