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Originally published In Press as doi:10.1074/jbc.M206274200 on September 6, 2002

J. Biol. Chem., Vol. 277, Issue 48, 46273-46279, November 29, 2002
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Dynamics-modulated Biological Activity of Transforming Growth Factor beta 3*,

Eduard V. BocharovDagger §, Dmitry M. KorzhnevDagger ||, Marcel J. J. Blommers**Dagger Dagger , Tudor Arvinte**, Vladislav Yu. Orekhov, Martin Billeter§§, and Alexander S. ArsenievDagger

From the Dagger  Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, Moscow 117997, Russia, the ** Novartis Pharma AG, Basel CH-4002, Switzerland, the  Swedish NMR Center at Göteborg University, Box 465, 405 30 Göteborg, Sweden, and the §§ Göteborg University, Lundberg Laboratory, Biochemistry and Biophysics, Box 462, 405 30 Göteborg, Sweden

Transforming growth factor beta 3 (TGF-beta 3) is an important mediator of growth, maintenance, and repair processes in human cells. Internal dynamic properties have been derived from 15N NMR relaxation data and mapped onto the spatial structure of TGF-beta 3. The pattern of internal dynamics in the structure identifies potential "hot spots" of binding free energy and reveals the importance of conformational entropy in the interaction of TGF-beta 3 with the receptors. The observed internal dynamics set TGF-beta 3 apart from other TGF-beta isoforms, with which it shares the same fold. These findings may explain functional differences among the various TGF-beta isoforms and thus prove essential in the search for related therapeutic agents.

* This work was supported by a grant from the Russian Foundation of Basic Research and a grant from the Royal Swedish Academy of Sciences.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 on-line version of this article (available at http://www.jbc.org) contains tables with 15N relaxation data (R1, R2, and 15N{1H} NOE), optimized model-free parameters (Sf2, Ss2, tau f, tau s, and Rex quantified at 11.7 T), and a detailed description of their confidence limits and two figures illustrating selection of the sample conditions and Rex values calculated as suggested in Ref. 45.

§ E. V. B. personally thanks K. A. Beirit for financial support.

|| Present address: Dept. Medical Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Dagger Dagger To whom correspondence should be addressed. Tel.: 41-61-3249064; Fax: 41-61-3242686; E-mail: marcel_jj.blommers@pharma.novartis.com.

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