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J. Biol. Chem., Vol. 283, Issue 6, 3002-3005, February 8, 2008

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Crystal Structure of the Human Laminin Receptor Precursor^*

Kelly V. Jamieson, Jinhua Wu, Stevan R. Hubbard¹, and Daniel Meruelo²

From the Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, New York, New York 10016 and the Structural Biology Program, Kimmel Center for Biology and Medicine of the Skirball Institute, and Department of Pharmacology, New York University School of Medicine, New York, New York 10016

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.

Received for publication, October 31, 2007 , and in revised form, November 13, 2007.

^* This work was supported by U. S. Public Health Service Grants CA100687 and CA68498 (to D. M.) and by grants from the NCI, National Institutes of Health and the Department of Health and Human Services. Some of the authors have competing interests. Specifically, the contents of this study are being utilized for a patent. According to the rules and regulations of New York University School of Medicine, if this patent is licensed by a third party, some of the authors (D. M., S. H., K. J.) may receive benefits in the form of royalties or equity participation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (code 3BCH) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

The on-line version of this article (available at http://www.jbc.org) contains two supplemental figures.

¹ The recipient of an Irma T. Hirschl-Monique Weill-Caulier Career Scientist Award. To whom correspondence may be addressed: Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Ave., New York, NY 10016. Tel.: 212-263-8938; Fax: 212-263-8951; E-mail: hubbard{at}saturn.med.nyu.edu. ² To whom correspondence may be addressed: Dept. of Pathology, New York University School of Medicine, 550 First Ave., New York, NY 10016. Tel.: 212-263-5599; Fax: 212-263-8211; E-mail: daniel.meruelo{at}med.nyu.edu.

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