https://scholars.lib.ntu.edu.tw/handle/123456789/372128
標題: | Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-like fold with a redox-active motif. | 作者: | TANG-LONG SHEN CHUN-HUA HSU |
公開日期: | 2012 | 摘要: | The novel tumor biomarker MIEN1, identified by representational difference analysis, is overexpressed in breast cancer and prostate cancer. MIEN1 is considered an oncogenic protein, because MIEN1 overexpression functionally enhances migration and invasion of tumor cells via modulating the activity of AKT. However, the structure and molecular function of MIEN1 is little understood. Here, we report the solution structure of MIEN1, which adopts a thioredoxin-like fold with a redox-active motif. Comparison of backbone chemical shifts showed that most of the residues for both oxidized and reduced MIEN1 possessed the same backbone conformation, with differences limited to the active motif and regions in proximity. The redox potential of this disulfide bond was measured as -225 mV, which compares well with that of disulfides for other thioredoxin-like proteins. Overall, our results suggest that MIEN1 may have an important regulatory role in phosphorylation of AKT with its redox potential. ? 2012 Hsu et al. |
URI: | http://europepmc.org/abstract/med/23284973 http://scholars.lib.ntu.edu.tw/handle/123456789/372128 |
DOI: | 10.1371/journal.pone.0052292 | SDG/關鍵字: | disulfide; migration and invasion enhancer 1 protein; oncoprotein; thioredoxin; unclassified drug; article; disulfide bond; oxidation reduction potential; protein conformation; protein folding; protein function; protein motif; protein secondary structure; protein structure; thermostability; Amino Acid Sequence; Circular Dichroism; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Nuclear Proteins; Oxidation-Reduction; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Thioredoxins; Transcription Factors |
顯示於: | 植物病理與微生物學系 |
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