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Protein Domain : IPR019825

Description  Lectins are carbohydrate-binding proteins. Leguminous lectins form one of the largest lectin families and resemble each other in their physicochemical properties, though they differ in their carbohydrate specificities. They bind either glucose/mannose or galactose [ ]. Carbohydrate-binding activity depends on the simultaneous presence of both a calcium and a transition metal ion []. The exact function of legume lectins is not known, but they may be involved in the attachment of nitrogen-fixing bacteria to legumes and in the protection against pathogens [, ].Some legume lectins are proteolytically processed to produce two chains, beta (which corresponds to the N-terminal) and alpha (C-terminal) [ ]. The lectin concanavalin A (conA) from jack bean is exceptional in that the two chains are transposed and ligated (by formation of a new peptide bond). The N terminus of mature conA thus corresponds to that of the alpha chain and the C terminus to the beta chain []. Though the legume lectins monomer is structurally well conserved, their quaternary structures vary widely [].The signature pattern for this entry is located in the C-terminal section of the beta chain and contains a conserved aspartic acid residue important for the binding of calcium and manganese. Name  Legume lectin, beta chain, Mn/Ca-binding site
Short Name  Lectin_legB_Mn/Ca_BS Type  Binding_site
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Genomics

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48 Protein Domain Regions