Kiewitz, Sebastian D. and Kruppa, Michael and Riechers, Alexander and Koenig, Burkhard and Cabrele, Chiara (2008) Recognition of the Helix-Loop-Helix domain of the Id proteins by an artificial luminescent metal complex receptor. JOURNAL OF MOLECULAR RECOGNITION, 21 (2). pp. 79-88. ISSN 0952-3499,
Full text not available from this repository. (Request a copy)Abstract
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) climerization 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 similar to 2 mu M 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. Copyright (c) 2008 John Wiley & Sons, Ltd.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CRYSTAL-STRUCTURE; BETA-PEPTIDE; DNA-BINDING; CANCER; WATER; TRANSCRIPTION; FAMILY; PERSPECTIVES; DIPEPTIDES; INHIBITORS; 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 |
| Divisions: | Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König Chemistry and Pharmacy > Institut für Organische Chemie > Alumni or Retired Professors > Arbeitskreis Dr. Chiara Cabrele |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 Nov 2020 05:43 |
| Last Modified: | 09 Nov 2020 05:43 |
| URI: | https://pred.uni-regensburg.de/id/eprint/31285 |
Actions (login required)
 |
View Item |
