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

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Item Type:	Article
Title:	LG/LNS domains: multiple functions - one business end?
Creators Name:	Rudenko, G., Hohenester, E. and Muller, Y.A.
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.
Keywords:	Amino Acid Sequence, Amino Acid Sequence Homology, Binding Sites, Laminin, Molecular Models, Molecular Sequence Data, Protein Conformation
Source:	Trends in Biochemical Sciences
ISSN:	0968-0004
Publisher:	Elsevier
Volume:	26
Number:	6
Page Range:	363-368
Date:	1 January 2001
Official Publication:	https://doi.org/10.1016/S0968-0004(01)01832-1
PubMed:	View item in PubMed

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