Diversity in recognition of glycans by F-type lectins and galectins: molecular, structural, and biophysical aspects.

ABSTRACT: Although lectins are "hard-wired" in the germline, the presence of tandemly arrayed carbohydrate recognition domains (CRDs), of chimeric structures displaying distinct CRDs, of polymorphic genes resulting in multiple isoforms, and in some cases, of a considerable recognition plasticity of their carbohydrate binding sites, significantly expand the lectin ligand-recognition spectrum and lectin functional diversification. Analysis of structural/functional aspects of galectins and F-lectins-the most recently identified lectin family characterized by a unique CRD sequence motif (a distinctive structural fold) and nominal specificity for l-Fuc-has led to a greater understanding of self/nonself recognition by proteins with tandemly arrayed CRDs. For lectins with a single CRD, however, recognition

SUBMITTER: Vasta GR 

PROVIDER: S-EPMC3683447 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature