title: LG/LNS domains: multiple functions -- one business end?
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.
authors.affiliation: Howard Hughes Medical Institute and Dept of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, USA. rudenko@chop.swmed.edu
authors.forename: G
authors.initials: G
authors.lastname: Rudenko
authors.forename: E
authors.initials: E
authors.lastname: Hohenester
authors.forename: Y A
authors.initials: YA
authors.lastname: Muller
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D007797:Laminin / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D007797:Laminin