| Literature DB >> 18063583 |
Kelly V Jamieson1, Jinhua Wu2, Stevan R Hubbard3, Daniel Meruelo4.
Abstract
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.Entities:
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Year: 2007 PMID: 18063583 DOI: 10.1074/jbc.C700206200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157