Kiewitz, S.D. and Kruppa, M. and Riechers, A. and König, B. and Cabrele, C. (2008) Recognition of the Helix-Loop-Helix Domain of the Id Proteins by an Artificial Luminescent Metal Complex Receptor. J. Mol. Recognit 21, 79 - 88.
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Synthetic agents specifically interacting with a protein interface are important not only for the better understanding of protein dimer or complex formation but also for medical applications. Here we describe the recognition of the helix-loop-helix (HLH) dimerization domain of the Id proteins by an artificial luminescent receptor containing two binding sites for a Lewis acid and a Lewis base, respectively. The Id proteins are inhibitors of bHLH transcription factors and play key roles during development of cancer. We show that a receptor/Id-HLH-domain complex was formed cooperatively (K(0.5) approximately 2 microM under physiological conditions) and with moderate specificity, as compared to the related MyoD and Max HLH domains. Accordingly, a preferred receptor binding motif, CYSR(K), was identified within the Id HLH domains. These results are promising and may be exploited to design highly selective synthetic receptors for the Id HLH domain.
|Institutions:|| Chemistry and Pharmacy > Institut für Organische Chemie > Arbeitskreis Dr. Chiara Cabrele|
Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König
|Projects:||GRK 760, Graduiertenkolleg Medizinische Chemie|
|Keywords:||Id proteins; protein domain recognition; helix-loop-helix; synthetic receptor; metal complex; crown ether; fluorescence spectroscopy; circular dichroism spectroscopy|
|Subjects:||500 Science > 540 Chemistry & allied sciences|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited On:||05 Mar 2009 10:55|
|Last Modified:||08 Nov 2010 13:18|