1IS6
MES-Liganded Congerin II
1IS6 の概要
| エントリーDOI | 10.2210/pdb1is6/pdb |
| 関連するPDBエントリー | 1C1L 1IS3 1IS4 1IS5 |
| 分子名称 | Congerin II, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total) |
| 機能のキーワード | mes complex, beta sandwich, sugar binding protein |
| 由来する生物種 | Conger myriaster (whitespotted conger) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15549.36 |
| 構造登録者 | Shirai, T.,Matsui, Y.,Shionyu-Mitsuyama, C.,Yamane, T.,Kamiya, H.,Ishii, C.,Ogawa, T.,Muramoto, K. (登録日: 2001-11-12, 公開日: 2002-09-18, 最終更新日: 2024-04-03) |
| 主引用文献 | Shirai, T.,Matsui, Y.,Shionyu-Mitsuyama, C.,Yamane, T.,Kamiya, H.,Ishii, C.,Ogawa, T.,Muramoto, K. Crystal structure of a conger eel galectin (congerin II) at 1.45 A resolution: Implication for the accelerated evolution of a new ligand-binding site following gene duplication J.MOL.BIOL., 321:879-889, 2002 Cited by PubMed Abstract: The crystal structure of congerin II, a galectin family lectin from conger eel, was determined at 1.45A resolution. The previously determined structure of its isoform, congerin I, had revealed a fold evolution via strand swap; however, the structure of congerin II described here resembles other prototype galectins. A comparison of the two congerin genes with that of several other galectins suggests acceralated evolution of both congerin genes following gene duplication. The presence of a Mes (2-[N-morpholino]ethanesulfonic acid) molecule near the carbohydrate-binding site in the crystal structure points to the possibility of an additional binding site in congerin II. The binding site consists of a group of residues that had been replaced following gene duplication suggesting that the binding site was built under selective pressure. Congerin II may be a protein specialized for biological defense with an affinity for target carbohydrates on parasites' cell surface. PubMed: 12206768DOI: 10.1016/S0022-2836(02)00700-3 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






