1IS4
LACTOSE-LIGANDED CONGERIN II
Summary for 1IS4
| Entry DOI | 10.2210/pdb1is4/pdb |
| Related | 1C1L 1IS3 1IS5 1IS6 |
| Related PRD ID | PRD_900004 |
| Descriptor | CONGERIN II, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | complex with lactose, beta sandwich, sugar binding protein |
| Biological source | Conger myriaster (whitespotted conger) |
| Total number of polymer chains | 1 |
| Total formula weight | 15696.42 |
| 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: 2024-04-03) |
| 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 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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