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Title: Crystal Structure of the Human Laminin Receptor Precursor

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.

Authors:
; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959580
Report Number(s):
BNL-82566-2009-JA
Journal ID: ISSN 0021-9258; JBCHA3; TRN: US201016%%724
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
Journal of Biological Chemistry
Additional Journal Information:
Journal Volume: 283; Journal Issue: 6; Journal ID: ISSN 0021-9258
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; DESIGN; DISEASES; POLYPHENOLS; PRECURSOR; TUMOR CELLS; LIGANDS; NEOPLASMS; national synchrotron light source

Citation Formats

Jamieson,K., Wu, J., Hubbard, S., and Meruelo, D. Crystal Structure of the Human Laminin Receptor Precursor. United States: N. p., 2008. Web. doi:10.1074/jbc.C700206200.
Jamieson,K., Wu, J., Hubbard, S., & Meruelo, D. Crystal Structure of the Human Laminin Receptor Precursor. United States. doi:10.1074/jbc.C700206200.
Jamieson,K., Wu, J., Hubbard, S., and Meruelo, D. Tue . "Crystal Structure of the Human Laminin Receptor Precursor". United States. doi:10.1074/jbc.C700206200.
@article{osti_959580,
title = {Crystal Structure of the Human Laminin Receptor Precursor},
author = {Jamieson,K. and Wu, J. and Hubbard, S. and Meruelo, D.},
abstractNote = {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.},
doi = {10.1074/jbc.C700206200},
journal = {Journal of Biological Chemistry},
issn = {0021-9258},
number = 6,
volume = 283,
place = {United States},
year = {2008},
month = {1}
}