C-Type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence

Glycobiology. 1999 Dec;9(12):1357-69. doi: 10.1093/glycob/9.12.1357.

Abstract

Protein modules related to the C-type carbohydrate-recognition domains of animal lectins are found in at least 125 proteins encoded in the Caenorhabditis elegans genome. Within these proteins, 183 C-type lectin-like domains (CTLDs) have been identified. The proteins have been classified based on the overall arrangement of modules within the polypeptides and based on sequence similarity between the CTLDs. The C.elegans proteins generally have different domain organization from known mammalian proteins containing CTLDs. Most of the CTLDs are divergent in sequence from those in mammalian proteins. However, 19 show conservation of most of the amino acid residues that ligate Ca(2+)to form a carbohydrate-binding site in vertebrate C-type carbohydrate-recognition domains. Seven of these domains are particularly similar in sequence to mannose- and N-acetylglucosamine-binding domains in the vicinity of this Ca(2+)site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Asialoglycoprotein Receptor
  • Binding Sites
  • Biological Evolution
  • Caenorhabditis elegans / chemistry*
  • Calcium / metabolism
  • Carrier Proteins / chemistry*
  • Collectins
  • Disulfides / chemistry
  • Galactose / metabolism
  • Lectins / metabolism*
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Receptors, Cell Surface / metabolism
  • Sequence Homology

Substances

  • Asialoglycoprotein Receptor
  • Carrier Proteins
  • Collectins
  • Disulfides
  • Lectins
  • Proteins
  • Receptors, Cell Surface
  • Calcium
  • Galactose