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Originally published In Press as doi:10.1074/jbc.M109453200 on December 14, 2001

J. Biol. Chem., Vol. 277, Issue 9, 6967-6973, March 1, 2002
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The PDZ1 Domain of SAP90
CHARACTERIZATION OF STRUCTURE AND BINDING*

Andrea PiserchioDagger , Maria Pellegrini§, Sunil Mehta§, Scott M. Blackman§, Elizabeth P. Garcia§, John Marshall§, and Dale F. MierkeDagger §

From the Dagger  Department of Chemistry and § Department of Molecular Pharmacology, Division of Biology and Medicine, Brown University, Providence, Rhode Island 02912

The structural features of the PDZ1 domain of the synapse-associated protein SAP90 have been characterized by NMR. A comparison with the structures of the PDZ2 and PDZ3 domains of SAP90 illustrates significant differences, which may account for the unique binding properties of these homologous domains. Within the postsynaptic density, SAP90 functions as a molecular scaffold with a number of the protein-protein interactions mediated through the PDZ1 domain. Here, using fluorescence anisotropy and NMR chemical shift analysis, we have characterized the association of PDZ1 to the C-terminal peptides of the GluR6 subunit of the kainate receptor, voltage-gated K+ channel Kv1.4, and microtubule-associate protein CRIPT, all of which are known to associate with SAP90. The latter two, which possess the consensus sequence for binding to PDZ domains (T/S-X-V-oh), have low micromolar binding affinities (1.5-15 µM). The C terminus of GluR6, RLPGKETMA-oh, lacking the consensus sequence, binds to PDZ1 of SAP90 with an affinity of 160 µM. The NMR data illustrate that although all three peptides occupy the binding groove capped by the GLGF loop of PDZ1, specific differences are present, consistent with the variation in binding affinities.

* This work was supported in part by National Institutes of Health Grants NS-39309 (to J. M.) and RR-15578 (to J. M. and D. F. M.).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 the structure factors (code 1KEF) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

To whom correspondence may be addressed: Dept. of Molecular Pharmacology, Division of Biology and Medicine, Box G-B4, Brown University, Providence, RI 02912. Tel.: 401-863-2139 (D. F. M.) or 401-863-2574 (J. M.); Fax: 401-863-1595; E-mail: dale_mierke@brown.edu (D. F. M.) or john_marshall{at}brown.edu (J. M.).

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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