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CASH - a beta-helix domain widespread among carbohydrate-binding proteins

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Creators Name:Ciccarelli, F.D. and Copley, R.R. and Doerks, T. and Russell, R.B. and Bork, P.
Journal Title:Trends in Biochemical Sciences
Journal Abbreviation:Trends Biochem Sci
Volume:27
Number:2
Page Range:59-62
Date:1 January 2002
Keywords:Amino Acid Motifs, Binding Sites, Carbohydrate Metabolism, Carrier Proteins, Polysaccharide-Lyases, Protein Folding, Secondary Protein Structure, Tertiary Protein Structure, Animals
Abstract:In this article, we describe a novel, widespread domain (CASH) that is shared by many carbohydrate-binding proteins and sugar hydrolases. This domain occurs in more than 1000 proteins distributed among all three kingdoms of life. The CASH domain is characterized by internal repetitions of glycines and hydrophobic residues that correspond to the repetitive units of a predicted or observed right-handed β-helix structure of the pectate lyase superfamily.
ISSN:0968-0004
Publisher:Elsevier (The Netherlands)
Item Type:Article

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