A novel cell binding site in the coiled-coil domain of laminin involved in capillary morphogenesis.

ABSTRACT: Recently, we reported the isolation and characterization of an anti-laminin antibody that modulates the extracellular matrix-dependent morphogenesis of endothelial cells. Here we use this antibody to precisely map the binding site responsible for mediating this biologically important interaction. By using a phage display-assisted mapping strategy to preserve protein structure, we demonstrate for the first time that the coiled-coil region of laminin contains a cell binding site. The adhesion motif is formed by residues contributed by both alpha and gamma chains, and is located in the middle part of the rod-like portion in a highly flexible area, which corresponds to a protease-susceptible site. Based on this information, a peptide mimotope was used to characterize the cognate receptor. Alth

SUBMITTER: Sanz L 

PROVIDER: S-EPMC152894 | biostudies-literature | 2003 Apr

REPOSITORIES: biostudies-literature