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Crystal structure of the human laminin receptor precursor.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2008 Feb 08; Vol. 283 (6), pp. 3002-3005. Date of Electronic Publication: 2007 Dec 06. - Publication Year :
- 2008
-
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.
- Subjects :
- Amino Acid Sequence
Animals
Caenorhabditis elegans
Crystallography, X-Ray
Humans
Ligands
Models, Molecular
Molecular Conformation
Molecular Sequence Data
Protein Binding
Receptors, Cell Surface chemistry
Saccharomyces cerevisiae
Sequence Homology, Amino Acid
Protein Precursors chemistry
Receptors, Laminin chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 283
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 18063583
- Full Text :
- https://doi.org/10.1074/jbc.C700206200