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Originally published In Press as doi:10.1074/jbc.C200571200 on November 19, 2002

J. Biol. Chem., Vol. 278, Issue 3, 1399-1402, January 17, 2003
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ACCELERATED PUBLICATION
Novel Mode of Ligand Recognition by the Erbin PDZ Domain*

Gabriel Birrane, Judy Chung, and John A. A. LadiasDagger

From the Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Division of Experimental Medicine, Harvard Institutes of Medicine, Harvard Medical School, Boston, Massachusetts 02115

Erbin contains a class I PDZ domain that binds to the C-terminal region of the receptor tyrosine kinase ErbB2, a class II ligand. The crystal structure of the human Erbin PDZ bound to the peptide EYLGLDVPV corresponding to the C-terminal residues 1247-1255 of human ErbB2 has been determined at 1.25-Å resolution. The Erbin PDZ deviates from the canonical PDZ fold in that it contains a single alpha -helix. The isopropyl group of valine at position -2 of the ErbB2 peptide interacts with the Erbin Val1351 and displaces the peptide backbone away from the alpha -helix, elucidating the molecular basis of class II ligand recognition by a class I PDZ domain. Strikingly, the phenolic ring of tyrosine -7 enters into a pocket formed by the extended beta 2-beta 3 loop of the Erbin PDZ. Phosphorylation of tyrosine -7 abolishes this interaction but does not affect the binding of the four C-terminal peptidic residues to PDZ, as revealed by the crystal structure of the Erbin PDZ complexed with a phosphotyrosine-containing ErbB2 peptide. Since phosphorylation of tyrosine -7 plays a critical role in ErbB2 function, the selective binding and sequestration of this residue in its unphosphorylated state by the Erbin PDZ provides a novel mechanism for regulation of the ErbB2-mediated signaling and oncogenicity.

* This work was supported by grants from the National Institutes of Health, the Massachusetts Department of Public Health, and the United States Department of Defense (to J. A. A. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The 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 (codes 1MFG and 1MFL) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Dagger Established Investigator of the American Heart Association. To whom correspondence should be addressed: Molecular Medicine Laboratory, Harvard Institutes of Medicine, Rm. 354, 4 Blackfan Circle, Boston, MA 02115. E-mail: jladias@caregroup.harvard.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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