X-ray crystal structures of animal lectins.
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.
Rini
J M
JM
Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.
D000818:Animals; D001665:Binding Sites; D002236:Carbohydrate Conformation; D002352:Carrier Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D016222:Fibroblast Growth Factor 2 / Q000737:chemistry / Q000378:metabolism; D006388:Hemagglutinins / Q000737:chemistry; D006801:Humans; D037102:Lectins / Q000737:chemistry*; D037241:Mannose-Binding Lectins; D008958:Models, Molecular; D011487:Protein Conformation; D051381:Rats
D002352:Carrier Proteins; D006388:Hemagglutinins; D037102:Lectins; D037241:Mannose-Binding Lectins; D016222:Fibroblast Growth Factor 2