A molecular model of the carbohydrate recognition domain of a rat macrophage lectin and analysis of its binding site.
A three-dimensional model of the carbohydrate recognition domain of a rat macrophage C-type lectin has been constructed by comparative modeling and assessed by inverse folding analysis. Comparative modeling in the presence of low sequence similarity was based on information provided by comparison of X-ray structures and sequence-structure alignments. The sequence-structure compatibility of the model was sound. Its binding site was analyzed in comparison to the X-ray structure of a galactose-specific mutant of the mannose-binding protein. The specificity of the macrophage lectin was discussed in light of mutagenesis data on asialoglycoprotein receptors.
Bajorath
J
J
Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121, USA.
D000818:Animals; D001665:Binding Sites / Q000235:genetics; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D003196:Computer Graphics; D006801:Humans; D037102:Lectins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008264:Macrophages / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism; D037241:Mannose-Binding Lectins; D008958:Models, Molecular; D015394:Molecular Structure; D009154:Mutation; D011487:Protein Conformation; D051381:Rats; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D037102:Lectins; D037241:Mannose-Binding Lectins; D008358:Mannose