Crystal Structure of the Human Laminin Receptor Precursor

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. He...

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Bibliographic Details
Published in:The Journal of biological chemistry 2008-02, Vol.283 (6), p.3002-3005
Main Authors: Jamieson, Kelly V., Wu, Jinhua, Hubbard, Stevan R., Meruelo, Daniel
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Caenorhabditis elegans
CRYSTAL STRUCTURE
Crystallography, X-Ray
DESIGN
DISEASES
Humans
LIGANDS
MATERIALS SCIENCE
Models, Molecular
Molecular Conformation
Molecular Sequence Data
national synchrotron light source
NEOPLASMS
POLYPHENOLS
PRECURSOR
Protein Binding
Protein Precursors - chemistry
Receptors, Cell Surface - chemistry
Receptors, Laminin - chemistry
Saccharomyces cerevisiae
Sequence Homology, Amino Acid
Sindbis virus
TUMOR CELLS
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.C700206200