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- W2080407828 abstract "The three-dimensional structures of LG/LNS domains from neurexin, the laminin alpha 2 chain and sex hormone-binding globulin reveal a close structural relationship to the carbohydrate-binding pentraxins and other lectins. However, these LG/LNS domains appear to have a preferential ligand-interaction site distinct from the carbohydrate-binding sites found in lectins, and this interaction site accommodates not only sugars but also steroids and proteins. In fact, the LG/LNS domain interaction site has features reminiscent of the antigen-combining sites in immunoglobulins. The LG/LNS domain presents an interesting case in which the fold has remained conserved but the functional sites have evolved; consequently, making predictions of structure-function relationships on the basis of the lectin fold alone is difficult." @default.
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- W2080407828 date "2001-06-01" @default.
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- W2080407828 title "LG/LNS domains: multiple functions – one business end?" @default.
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- W2080407828 doi "https://doi.org/10.1016/s0968-0004(01)01832-1" @default.
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