title: Expression and characterization of a carbohydrate-binding fragment of rat aggrecan.
abstract: The COOH-terminal portion of cartilage proteoglycan core protein, aggrecan, expressed by in vitro translation, binds carbohydrate-containing affinity columns. The in vitro expression approach has been used to define the sugar-binding portion of the core protein. The active fragment, which corresponds closely to the carbohydrate-recognition domains in the family of Ca(2+)-dependent (C-type) animal lectins, has been expressed in bacteria and characterized. The CD spectrum of the domain is very similar to the spectrum of the binding domain of serum mannose-binding protein, suggesting that its overall structure probably resembles the known three-dimensional structure of the mannose-binding domain. The binding specificity of the core protein fragment has been characterized using a solid-phase assay. The results suggest that the monosaccharide-binding site is also similar to that in other C-type carbohydrate-recognition domains.
authors: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
authors: S
authors: S
authors: Saleque
authors: N
authors: N
authors: Ruiz
authors: K
authors: K
authors: Drickamer
mesh_terms: D053674:Aggrecans; D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000235:genetics; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D004247:DNA / Q000235:genetics; D016326:Extracellular Matrix Proteins; D015870:Gene Expression; D006801:Humans; D037181:Lectins, C-Type; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D014176:Protein Biosynthesis; D011509:Proteoglycans / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
chemical_list: C508321:Acan protein, rat; D053674:Aggrecans; D016326:Extracellular Matrix Proteins; D037181:Lectins, C-Type; D010446:Peptide Fragments; D011509:Proteoglycans; D004247:DNA