1IS4

LACTOSE-LIGANDED CONGERIN II

1IS4 の概要

• エントリーDOI: 10.2210/pdb1is4/pdb
• 関連するPDBエントリー: 1C1L 1IS3 1IS5 1IS6
• 関連するBIRD辞書のPRD_ID: PRD_900004
• 分子名称: CONGERIN II, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: complex with lactose, 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: 15696.42

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

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: 12206768
DOI: 10.1016/S0022-2836(02)00700-3

実験手法

X-RAY DIFFRACTION (1.9 Å)