LG/LNS domains: Multiple functions - One business end?

Gabby Rudenko, Erhard Hohenester, Yves A. Muller

Research output: Contribution to journalReview article

73 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)363-368
Number of pages6
JournalTrends in biochemical sciences
Volume26
Issue number6
DOIs
StatePublished - Jun 1 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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