2E6V
Crystal structure of VIP36 exoplasmic/lumenal domain, Ca2+/Man3GlcNAc-bound form
2E6V の概要
エントリーDOI | 10.2210/pdb2e6v/pdb |
関連するPDBエントリー | 1GV9 1R1Z 2DUO 2DUP 2DUQ 2DUR |
分子名称 | Vesicular integral-membrane protein VIP36, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose, CALCIUM ION, ... (5 entities in total) |
機能のキーワード | beta sandwich, carbohydrate binding protein, cargo receptor, protein transport |
由来する生物種 | Canis lupus familiaris (dog) |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 146046.01 |
構造登録者 | |
主引用文献 | Satoh, T.,Cowieson, N.P.,Hakamata, W.,Ideo, H.,Fukushima, K.,Kurihara, M.,Kato, R.,Yamashita, K.,Wakatsuki, S. Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36 J.Biol.Chem., 282:28246-28255, 2007 Cited by PubMed Abstract: VIP36 functions as a transport lectin for trafficking certain high mannose type glycoproteins in the secretory pathway. Here we report the crystal structure of VIP36 exoplasmic/luminal domain comprising a carbohydrate recognition domain and a stalk domain. The structures of VIP36 in complex with Ca(2+) and mannosyl ligands are also described. The carbohydrate recognition domain is composed of a 17-stranded antiparallel beta-sandwich and binds one Ca(2+) adjoining the carbohydrate-binding site. The structure reveals that a coordinated Ca(2+) ion orients the side chains of Asp(131), Asn(166), and His(190) for carbohydrate binding. This result explains the Ca(2+)-dependent carbohydrate binding of this protein. The Man-alpha-1,2-Man-alpha-1,2-Man, which corresponds to the D1 arm of high mannose type glycan, is recognized by eight residues through extensive hydrogen bonds. The complex structures reveal the structural basis for high mannose type glycoprotein recognition by VIP36 in a Ca(2+)-dependent and D1 arm-specific manner. PubMed: 17652092DOI: 10.1074/jbc.M703064200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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