1IS3

LACTOSE AND MES-LIGANDED CONGERIN II

Summary for 1IS3

• Entry DOI: 10.2210/pdb1is3/pdb
• Related: 1C1L 1IS4 1IS5 1IS6
• Related PRD ID: PRD_900004
• Descriptor: CONGERIN II, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: complex with lactose and mes, sugar binding protein
• Biological source: Conger myriaster (whitespotted conger)
• Total number of polymer chains: 1
• Total formula weight: 15891.65

Authors

Shirai, T.,Matsui, Y.,Shionyu-Mitsuyama, C.,Yamane, T.,Kamiya, H.,Ishii, C.,Ogawa, T.,Muramoto, K. (deposition date: 2001-11-12, release date: 2002-09-18, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.45 Å)