4TQM
Structural basis of specific recognition of non-reducing terminal N-acetylglucosamine by an Agrocybe aegerita lection
4TQM の概要
| エントリーDOI | 10.2210/pdb4tqm/pdb |
| 関連するPDBエントリー | 4TQJ 4TQK |
| 分子名称 | Lectin 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose, ... (4 entities in total) |
| 機能のキーワード | complex, lectin, glcnac, sugar binding protein |
| 由来する生物種 | Agrocybe aegerita (Black poplar mushroom) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 46398.35 |
| 構造登録者 | |
| 主引用文献 | Ren, X.M.,Li, D.F.,Jiang, S.,Lan, X.Q.,Hu, Y.,Sun, H.,Wang, D.C. Structural Basis of Specific Recognition of Non-Reducing Terminal N-Acetylglucosamine by an Agrocybe aegerita Lectin. Plos One, 10:e0129608-e0129608, 2015 Cited by PubMed Abstract: O-linked N-acetylglucosaminylation (O-GlcNAcylation) is a reversible post-translational modification that plays essential roles in many cellular pathways. Research in this field, however, is hampered by the lack of suitable probes to identify, accumulate, and purify the O-GlcNAcylated proteins. We have previously reported the identification of a lectin from the mushroom Agrocybe aegerita, i.e., Agrocybe aegerita lectin 2, or AAL2, that could bind terminal N-acetylglucosamine with higher affinities and specificity than other currently used probes. In this paper, we report the crystal structures of AAL2 and its complexes with GlcNAc and GlcNAcβ1-3Galβ1-4GlcNAc and reveal the structural basis of GlcNAc recognition by AAL2 and residues essential for the binding of terminal N-acetylglucosamine. Study on AAL2 may enable us to design a protein probe that can be used to identify and purify O-GlcNAcylated proteins more efficiently. PubMed: 26114302DOI: 10.1371/journal.pone.0129608 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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