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LG/LNS domains: multiple functions - one business end?

Official URL:https://doi.org/10.1016/S0968-0004(01)01832-1
PubMed:View item in PubMed
Creators Name:Rudenko, G. and Hohenester, E. and Muller, Y.A.
Journal Title:Trends in Biochemical Sciences
Journal Abbreviation:Trends Biochem Sci
Volume:26
Number:6
Page Range:363-368
Date:1 January 2001
Keywords:Amino Acid Sequence, Amino Acid Sequence Homology, Binding Sites, Laminin, Molecular Models, Molecular Sequence Data, Protein Conformation
Abstract:The three-dimensional structures of LG/LNS domains from neurexin, the laminin α2 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.
ISSN:0968-0004
Publisher:Elsevier (The Netherlands)
Item Type:Article

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