McIntosh, P.B. and Frenkiel, T.A. and Wellborn, U. and McCormick, J.E. and Klempnauer, K.H. and Feeney, J. and Carr, M.D. (1998) Solution structure of the B-Myb DNA-binding domain: A possible role for conformational instability of the protein in DNA binding and control of gene expression. Biochemistry, 37 (27). pp. 9619-9629. ISSN 0006-2960.
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Double- and triple-resonance heteronuclear NMR spectroscopy have been used to determine the high-resolution solution structure of the minimal B-Myb DNA-binding domain (B-MybR2R3) and to characterize the specific complex formed with a synthetic DNA fragment corresponding to the Myb target site on the Myb-regulated gene tom-1. B-MybR2R3 is shown to consist of two independent protein domains (R2 and R3) joined by a short linker, which have strikingly different tertiary structures despite significant sequence similarities, In addition, the C-terminal region of B-Myb R2 is confirmed to have a poorly defined structure, reflecting the existence of multiple conformations in slow to intermediate exchange. This contrasts with the tertiary structure reported for c-MybR2R3, in which both R2 and R3 have the same fold and the C-terminal region of R2 forms a stable, well-defined helix [Ogata, K., et al. (1995) Nat. Struct. Biol, 2, 309-320]. The NMR data suggest there are extensive contacts between B-MybR2R3 and its DNA target site in the complex and are consistent with a significant conformational change in the protein on binding to DNA, with one possibility being the formation of a stable helix in the C-terminal region of R2. In addition, conformational heterogeneity identified in R2 of B-MybR2R3 bound to the tom-1-A target site may play an important role in the control of gene expression by Myb proteins.
|Additional information:||his work was supported by the Medical Research Council (U.K.), the Department of Health (U.K.), and the Max-Planck Society (Germany). U.W. acknowledges the award of a postdoctoral fellowship from the Deutsche Forschungsgemeinschaft. , ‡ The coordinates of the 32 converged B-MybR2R3 structures, together with the experimental NMR constraints, have been deposited in the Brookhaven Protein Data Bank (PDB file names 1a5j and r1a5jmr, respectively). , § National Institute for Biological Standards and Control. , MRC Biomedical NMR Centre, National Institute for Medical Research. , Division of Molecular Structure, National Institute for Medical Research. , # Max Planck Institut für Immunbiologie. , * To whom correspondence should be addressed at Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, U.K. , @ University of Kent.|
Q Science > QD Chemistry
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||M.A. Ziai|
|Date Deposited:||22 Oct 2009 08:31|
|Last Modified:||22 Oct 2009 08:31|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/17447 (The current URI for this page, for reference purposes)|
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