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

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...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2001-06, Vol.26 (6), p.363-368
Main Authors: Rudenko, Gabby, Hohenester, Erhard, Muller, Yves A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
jelly-roll
Laminin - chemistry
Laminin - metabolism
Laminin G-like domain
legume lectin fold
LNS domain
Models, Molecular
Molecular Sequence Data
neurexin
Protein Conformation
Sequence Homology, Amino Acid
sex hormone-binding globulin
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Summary: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
1362-4326
DOI:10.1016/S0968-0004(01)01832-1