Ontology highlight
ABSTRACT:
SUBMITTER: Carafoli F
PROVIDER: S-EPMC2755686 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Carafoli Federico F Clout Naomi J NJ Hohenester Erhard E
The Journal of biological chemistry 20090624 34
Laminins are large heterotrimeric glycoproteins with many essential functions in basement membrane assembly and function. Cell adhesion to laminins is mediated by a tandem of five laminin G-like (LG) domains at the C terminus of the alpha chain. Integrin binding requires an intact LG1-3 region, as well as contributions from the coiled coil formed by the alpha, beta, and gamma chains. We have determined the crystal structure at 2.8-A resolution of the LG1-3 region of the laminin alpha2 chain (alp ...[more]