AI Article Synopsis
- The Ergp55 protein is an Ets family transcription factor, crucial for development and cancer metabolism, and its structure and DNA binding mechanisms were explored through biophysical techniques after production in E. coli.
- The study found that Ergp55 exhibits a high amount of α-helix and random coil structures, and its full-length form is flexible, with evidence of autoinhibition occurring in longer fragments of the protein.
- This research could help in creating compounds that stabilize the inactive form of Ergp55, providing a pathway for developing treatments targeting prostate cancer.
Article Abstract
Background: The Ergp55 protein belongs to Ets family of transcription factor. The Ets proteins are highly conserved in their DNA binding domain and involved in various development processes and regulation of cancer metabolism. To study the structure and DNA binding autoinhibition mechanism of Ergp55 protein, we have produced full length and smaller polypeptides of Ergp55 protein in E. coli and characterized using various biophysical techniques.
Results: The Ergp55 polypeptides contain large amount of α-helix and random coil structures as measured by circular dichorism spectroscopy. The full length Ergp55 forms a flexible and elongated molecule as revealed by molecular modeling, dynamics simulation and structural prediction algorithms. The binding analyses of Ergp55 polypeptides with target DNA sequences of E74 and cfos promoters indicate that longer fragments of Ergp55 (beyond the Ets domain) showed the evidence of auto-inhibition. This study also revealed the parts of Ergp55 protein that mediate auto-inhibition.
Significance: The current study will aid in designing the compounds that stabilize the inhibited form of Ergp55 and inhibit its binding to promoter DNA. It will contribute in the development of drugs targeting Ergp55 for the prostate cancer treatment.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386182 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0039850 | PLOS |
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Purification, crystallization and preliminary X-ray crystallographic analysis of the ETS domain of human Ergp55 in complex with the cfos promoter DNA sequence.
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The Ergp55 protein belongs to the Ets family of transciption factors. The Ets transcription factors are involved in various developmental processes and the regulation of cancer metabolism. They contain a highly similar DNA-binding domain known as the ETS domain and have diverse functions in oncogenesis and physiology.
View Article and Find Full Text PDFStructural modeling and DNA binding autoinhibition analysis of Ergp55, a critical transcription factor in prostate cancer.
PLoS One
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Article Synopsis
- The Ergp55 protein is an Ets family transcription factor, crucial for development and cancer metabolism, and its structure and DNA binding mechanisms were explored through biophysical techniques after production in E. coli.
- The study found that Ergp55 exhibits a high amount of α-helix and random coil structures, and its full-length form is flexible, with evidence of autoinhibition occurring in longer fragments of the protein.
- This research could help in creating compounds that stabilize the inactive form of Ergp55, providing a pathway for developing treatments targeting prostate cancer.
Erg proteins, transcription factors of the Ets family, form homo, heterodimers and ternary complexes via two distinct domains.
Oncogene
June 1998
CNRS UMR 319, Institut de Biologie de Lille, France.
The ets genes family encodes a group of proteins which function as transcription factors under physiological conditions. We report here that the Erg proteins, members of the Ets family, form homo and heterodimeric complexes in vitro. We demonstrate that the Ergp55 protein isoform forms dimers with itself and with the two other isoforms, Ergp49 and Ergp38.
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