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Recognition of the Helix-Loop-Helix domain of the Id proteins by an artificial luminescent metal complex receptor

✍ Scribed by Sebastian D. Kiewitz; Michael Kruppa; Alexander Riechers; Burkhard König; Chiara Cabrele

Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
399 KB
Volume
21
Category
Article
ISSN
0952-3499

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✦ Synopsis

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) 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~ ∼2 µM 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 © 2008 John Wiley & Sons, Ltd.

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