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Originally published In Press as doi:10.1074/jbc.C200139200 on March 19, 2002

J. Biol. Chem., Vol. 277, Issue 19, 16351-16354, May 10, 2002
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ACCELERATED PUBLICATION
A Direct Test of the Reductionist Approach to Structural Studies of Calmodulin Activity
RELEVANCE OF PEPTIDE MODELS OF TARGET PROTEINS*

James K. KranzDagger §, Eun K. LeeDagger , Angus C. Nairn, and A. Joshua WandDagger ||

From the Dagger  The Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059 and the  Laboratory of Molecular and Cellular Neurosciences, The Rockefeller University, New York, New York 10021

Ca2+-saturated calmodulin (CaM) directly associates with and activates CaM-dependent protein kinase I (CaMKI) through interactions with a short sequence in its regulatory domain. Using heteronuclear NMR 13C-15N-1H correlation experiments, the backbone assignments were determined for CaM bound to a peptide (CaMKIp) corresponding to the CaM-binding sequence of CaMKI. A comparison of chemical shifts for free CaM with those of the CaM·CaMKIp complex indicate large differences throughout the CaM sequence. Using NMR techniques optimized for large proteins, backbone resonance assignments were also determined for CaM bound to the intact CaMKI enzyme. NMR spectra of CaM bound to either the CaMKI enzyme or peptide are virtually identical, indicating that calmodulin is structurally indistinguishable when complexed to the intact kinase or the peptide CaM-binding domain. Chemical shifts of CaM bound to a peptide (smMLCKp) corresponding to the calmodulin-binding domain of smooth muscle myosin light chain kinase are also compared with the CaM·CaMKI complexes. Chemical shifts can differentiate one complex from another, as well as bound versus free states of CaM. In this context, the observed similarity between CaM·CaMKI enzyme and peptide complexes is striking, indicating that the peptide is an excellent mimetic for interaction of calmodulin with the CaMKI enzyme.

* This work was supported by National Institutes of Health (NIH) Grants DK39806 and GM50402 and by equipment grants from the NIH and the Army Research Office.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.

§ Recipient of National Research Service Award Fellowship GM20206.

|| To whom correspondence should be addressed: Dept. of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, PA 19104. Tel.: 215-573-7288; Fax: 215-573-7290; E-mail: wand@ mail.med.upenn.edu.

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


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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.