Kiewitz, Sebatsian D. and Cabrele, Chiara (2005) Synthesis and conformational properties of protein fragments based on the Id family of DNA-binding and cell-differentiation inhibitors. BIOPOLYMERS, 80 (6). pp. 762-774. ISSN 0006-3525, 1097-0282
Full text not available from this repository. (Request a copy)Abstract
Id proteins are dominant negative regulators of the helix-loop-helix (HLH) transcription factors and are important during development, especially by preventing cell differentiation while inducing cell proliferation. In contrast. they are poorly expressed in healthy adults but are found in several tumor types. The Id HLH motif is responsible for the inhibitory activity, whereas not much is known about the role of the N- and C-termini. In the presented work, synthetic peptides reproducing the HLH, the N-terminal region, and the C-terminal region of the Id proteins were characterized by CD. The four HLH sequences built highly stable helical conformations, whereas the N- and C-termini were unstructured, with the exception of art alanine-rich fragment preceding the ld4 HLH motif. Deletion of the loop connecting the two helices led to helix destabilization for all four ld HLH peptides. In addition, modifications of the amino acid composition within the hydrophobic face of the helices of the Id1 HLH peptide induced conformational changes, mostly associated with loss of helix content. Moreover, a fragment containing the helix-2 and the C-terminus of the ld1 protein did not show any helical character. Therefore, both the helix propensity and stability of the HLH domain were shown to be strongly dependent on favorable interhelical contacts. In contrast, it is suggested that the regions beyond this domain could rather play a destabilizing role, for example, by increasing the flexibility of the folded protein. (c) 2005 Wiley Periodicals, Inc.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | LOOP-HELIX PROTEINS; GUANIDINE-HYDROCHLORIDE; TRANSCRIPTION FACTORS; CIRCULAR-DICHROISM; FOLDING PROBLEM; EMPIRICAL PARAMETERS; CRYSTAL-STRUCTURE; ALPHA-HELICES; PH-DEPENDENCE; COILED-COILS; helix-loop-helix motif; DNA-binding inhibitors; Id proteins; CD |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Chemistry and Pharmacy > Institut für Organische Chemie > Alumni or Retired Professors > Arbeitskreis Dr. Chiara Cabrele |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 01 Jun 2021 15:10 |
| Last Modified: | 01 Jun 2021 15:10 |
| URI: | https://pred.uni-regensburg.de/id/eprint/36640 |
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