5AV7
Crystal structure of Calsepa lectin in complex with bisected glycan
5AV7 の概要
| エントリーDOI | 10.2210/pdb5av7/pdb |
| 関連するPDBエントリー | 5AVA |
| 分子名称 | Lectin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)][2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]methyl alpha-D-mannopyranoside (3 entities in total) |
| 機能のキーワード | lectin, glycan, sugar binding protein |
| 由来する生物種 | Calystegia sepium (Hedge bindweed) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 65746.23 |
| 構造登録者 | |
| 主引用文献 | Nagae, M.,Kanagawa, M.,Morita-Matsumoto, K.,Hanashima, S.,Kizuka, Y.,Taniguchi, N.,Yamaguchi, Y. Atomic visualization of a flipped-back conformation of bisected glycans bound to specific lectins Sci Rep, 6:22973-22973, 2016 Cited by PubMed Abstract: Glycans normally exist as a dynamic equilibrium of several conformations. A fundamental question concerns how such molecules bind lectins despite disadvantageous entropic loss upon binding. Bisected glycan, a glycan possessing bisecting N-acetylglucosamine (GlcNAc), is potentially a good model for investigating conformational dynamics and glycan-lectin interactions, owing to the unique ability of this sugar residue to alter conformer populations and thus modulate the biological activities. Here we analyzed bisected glycan in complex with two unrelated lectins, Calsepa and PHA-E. The crystal structures of the two complexes show a conspicuous flipped back glycan structure (designated 'back-fold' conformation), and solution NMR analysis also provides evidence of 'back-fold' glycan structure. Indeed, statistical conformational analysis of available bisected and non-bisected glycan structures suggests that bisecting GlcNAc restricts the conformations of branched structures. Restriction of glycan flexibility by certain sugar residues may be more common than previously thought and impinges on the mechanism of glycoform-dependent biological functions. PubMed: 26971576DOI: 10.1038/srep22973 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.85 Å) |
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