4YGC
Crystal structure of ERGIC-53/MCFD2, monoclinic calcium-bound form 1
4YGC の概要
エントリーDOI | 10.2210/pdb4ygc/pdb |
関連するPDBエントリー | 4YGB 4YGD 4YGE |
分子名称 | Protein ERGIC-53, Multiple coagulation factor deficiency protein 2, CALCIUM ION, ... (5 entities in total) |
機能のキーワード | beta-sandwich, ef-hand, cargo receptor, calcium binding, er, ergic, protein transport |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 157624.72 |
構造登録者 | Satoh, T.,Nishio, M.,Yagi-Utsumi, M.,Suzuki, K.,Anzai, T.,Mizushima, T.,Kamiya, Y.,Kato, K. (登録日: 2015-02-26, 公開日: 2016-04-06, 最終更新日: 2024-11-06) |
主引用文献 | Satoh, T.,Nishio, M.,Suzuki, K.,Yagi-Utsumi, M.,Kamiya, Y.,Mizushima, T.,Kato, K. Crystallographic snapshots of the EF-hand protein MCFD2 complexed with the intracellular lectin ERGIC-53 involved in glycoprotein transport. Acta Crystallogr.,Sect.F, 76:216-221, 2020 Cited by PubMed Abstract: The transmembrane intracellular lectin ER-Golgi intermediate compartment protein 53 (ERGIC-53) and the soluble EF-hand multiple coagulation factor deficiency protein 2 (MCFD2) form a complex that functions as a cargo receptor, trafficking various glycoproteins between the endoplasmic reticulum (ER) and the Golgi apparatus. It has been demonstrated that the carbohydrate-recognition domain (CRD) of ERGIC-53 (ERGIC-53) interacts with N-linked glycans on cargo glycoproteins, whereas MCFD2 recognizes polypeptide segments of cargo glycoproteins. Crystal structures of ERGIC-53 complexed with MCFD2 and mannosyl oligosaccharides have revealed protein-protein and protein-sugar binding modes. In contrast, the polypeptide-recognition mechanism of MCFD2 remains largely unknown. Here, a 1.60 Å resolution crystal structure of the ERGIC-53-MCFD2 complex is reported, along with three other crystal forms. Comparison of these structures with those previously reported reveal that MCFD2, but not ERGIC-53-CRD, exhibits significant conformational plasticity that may be relevant to its accommodation of various polypeptide ligands. PubMed: 32356523DOI: 10.1107/S2053230X20005452 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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