C-type lectin-like domains.
Carbohydrate-recognition domains of C-type (Ca2+-dependent) animal lectins serve as prototypes for an important family of protein modules. Only some domains in this family bind Ca2+ or sugars. A comparison of recent structures of C-type lectin-like domains reveals diversity in the modular fold, particularly in the region associated with Ca2+ and sugar binding. Some of this diversity reflects the changes that occur during normal physiological functioning of the domains. C-type lectin-like domains associate with each other through several different surfaces to form dimers and trimers, from which ligand-binding sites project in a variety of different orientations.
Drickamer
K
K
Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. kd@glycob.ox.ac.uk
D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D002118:Calcium / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
D037102:Lectins; D046911:Macromolecular Substances; D002118:Calcium