A novel cell binding site in the coiled-coil domain of laminin involved in capillary morphogenesis
AUTOR(ES)
Sanz, Laura
FONTE
Oxford University Press
RESUMO
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 α and γ 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. Although we can not rule out the implication of other receptors, our results demonstrate that the laminin helical rod active site interacts with α2β1 integrin on the surface of endothelial cells. These findings provide new insight into the complex mechanisms regulating capillary morphogenesis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=152894Documentos Relacionados
- Evidence for coiled-coil alpha-helical regions in the long arm of laminin.
- NuMA/centrophilin: sequence analysis of the coiled-coil rod domain.
- Crystallization of the coiled-coil domain of Atg16 essential for autophagy
- An Antiviral Peptide Targets a Coiled-Coil Domain of the Human T-Cell Leukemia Virus Envelope Glycoprotein
- Electron-transfer functionality of synthetic coiled-coil metalloproteins
