Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion

Glycobiology. 1995 Jun;5(4):435-41. doi: 10.1093/glycob/5.4.435.


The N-linked HNK-1 carbohydrate expressed by several recognition molecules mediates the adhesion of early post-natal cerebellar neurons to the G2 domain of the terminal globular domain of the laminin alpha 1 chain (H. Hall et al., submitted). To define this binding site more precisely, G2-derived synthetic peptides were used for binding and competition studies. Peptide 5-G2, comprising the amino acid residues 3431-3451 of G2, inhibited the interaction between the HNK-1-carrying glycolipid and laminin in a concentration-dependent and saturable manner. Peptides which overlap only partially with this sequence interfered less. Peptides comprising other amino acid sequences from G2, and peptides derived from G1 and G3 or a scrambled version of peptide 5-G2, did not show significant effects. Direct binding of peptide 5-G2 to the HNK-1 glycolipid was also demonstrated. Furthermore, peptide 5-G2 interfered in a concentration-dependent and saturable manner with the adhesion of early postnatal cerebellar neurons to laminin. These observations indicate that amino acid residues 3431-3451 of the laminin G2 domain are involved in HNK-1 carbohydrate-mediated cell adhesion.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Binding Sites
  • CD57 Antigens / metabolism*
  • Cell Adhesion* / drug effects
  • Cerebellum / cytology
  • Immunoglobulin Fab Fragments
  • Laminin / chemistry*
  • Laminin / metabolism*
  • Mice
  • Mice, Inbred ICR
  • Molecular Sequence Data
  • Neurons / metabolism
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism*
  • Peptide Fragments / pharmacology
  • Structure-Activity Relationship


  • Antibodies, Monoclonal
  • CD57 Antigens
  • Immunoglobulin Fab Fragments
  • Laminin
  • Peptide Fragments