Crystal structure of the human laminin receptor precursor
KV Jamieson, J Wu, SR Hubbard, D Meruelo - Journal of Biological …, 2008 - jbc.org
The human laminin receptor (LamR) interacts with many ligands, including laminin, prions,
Sindbis virus, and the polyphenol (–)-epigallocatechin-3-gallate (EGCG), and has been
implicated in a number of diseases. LamR is overexpressed on tumor cells, and targeting
LamR elicits anti-cancer effects. Here, we report the crystal structure of human LamR, which
provides insights into its function and should facilitate the design of novel therapeutics
targeting LamR.
Sindbis virus, and the polyphenol (–)-epigallocatechin-3-gallate (EGCG), and has been
implicated in a number of diseases. LamR is overexpressed on tumor cells, and targeting
LamR elicits anti-cancer effects. Here, we report the crystal structure of human LamR, which
provides insights into its function and should facilitate the design of novel therapeutics
targeting LamR.