[HTML][HTML] The LG1-3 tandem of laminin α5 harbors the binding sites of Lutheran/basal cell adhesion molecule and α3β1/α6β1 integrins
Y Kikkawa, T Sasaki, MT Nguyen, M Nomizu… - Journal of biological …, 2007 - ASBMB
The laminin-type globular (LG) domains of laminin α chains have been implicated in various
cellular interactions that are mediated through receptors such as integrins, α-dystroglycan,
syndecans, and the Lutheran blood group glycoprotein (Lu). Lu, an Ig superfamily
transmembrane receptor specific for laminin α5, is also known as basal cell adhesion
molecule (B-CAM). Although Lu/B-CAM binds to the LG domain of laminin α5, the binding
site has not been precisely defined. To better delineate this binding site, we produced a …
cellular interactions that are mediated through receptors such as integrins, α-dystroglycan,
syndecans, and the Lutheran blood group glycoprotein (Lu). Lu, an Ig superfamily
transmembrane receptor specific for laminin α5, is also known as basal cell adhesion
molecule (B-CAM). Although Lu/B-CAM binds to the LG domain of laminin α5, the binding
site has not been precisely defined. To better delineate this binding site, we produced a …