Crystal structure of the human laminin receptor precursor

J Biol Chem. 2008 Feb 8;283(6):3002-3005. doi: 10.1074/jbc.C700206200. Epub 2007 Dec 6.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans
  • Crystallography, X-Ray
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Protein Binding
  • Protein Precursors / chemistry*
  • Receptors, Cell Surface / chemistry
  • Receptors, Laminin / chemistry*
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid

Substances

  • Ligands
  • Protein Precursors
  • Receptors, Cell Surface
  • Receptors, Laminin

Associated data

  • PDB/3BCH