X-ray crystal structures of animal lectins

Abstract

Several important advances in the structure determination of animal lectins were made in the past year. The X-ray crystal structures of trimeric fragments of the human and rat mannose-binding proteins have defined for the first time the three-dimensional subunit organization of a multimeric C-type lectin. In addition, the structure of a galectin-biantennary oligosaccharide complex has provided a model for what might be biochemically relevant cross-linking interactions. Finally, in a novel variation on lectin cross-linking, independent carbohydrate-binding sites on basic fibroblast growth factor have been found to recognize opposing faces of a synthetic heparin/heparan sulphate fragment, leading to growth-factor polymerization.