TY - JOUR
T1 - Crystal structure of the human laminin receptor precursor
AU - Jamieson, Kelly V.
AU - Wu, Jinhua
AU - Hubbard, Stevan R.
AU - Meruelo, Daniel
PY - 2008/2/8
Y1 - 2008/2/8
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=41249088465&partnerID=8YFLogxK
U2 - 10.1074/jbc.C700206200
DO - 10.1074/jbc.C700206200
M3 - Article
C2 - 18063583
AN - SCOPUS:41249088465
SN - 0021-9258
VL - 283
SP - 3002
EP - 3005
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 6
ER -
