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Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: Application to cGMP-dependent protein kinase I

¹ Department of Biological Chemistry and Molecular Pharmacology and ² Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02115, USA
³ Department of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany

(RECEIVED April 19, 2005; FINAL REVISION June 7, 2005; ACCEPTED June 21, 2005)

Coiled-coil motifs play essential roles in protein assembly and molecular recognition, and are therefore the targets of many ongoing structural and functional studies. However, owing to the dynamic nature of many of the smaller coiled-coil domains, crystallization for X-ray studies is very challenging. Determination of elongated structures using standard NMR approaches is inefficient and usually yields low-resolution structures due to accumulation of small errors over long distances. Here we describe a solution NMR approach based on residual dipolar couplings (RDCs) for rapid and accurate structure determination of coiled-coil dimers. Using this approach, we were able to determine the high-resolution structure of the coiled-coil domain of cGMP-dependent protein kinase I, a protein of previously unknown structure that is critical for physiological relaxation of vascular smooth muscle. This approach can be extended to solve coiled-coil structures with higher order assemblies.

Keywords: coiled coil; residual dipolar coupling; NMR; cGMP-dependent protein kinase I

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051528905.

Reprint requests to: James J. Chou, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; e-mail: james_chou{at}hms.harvard.edu; fax: (617) 432-2921.

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