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A PROSS-designed extensively mutated estrogen receptor α variant displays enhanced thermal stability while retaining native allosteric regulation and structure
Protein stability limitations often hamper the exploration of proteins as drug targets. Here, we show that the application of PROSS server algorithms to the ligand-binding domain of human estrogen receptor alpha (hERα) enabled the development of variant ER(PRS*) that comprises 24 amino acid substitu...
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| 出版年: | Sci Rep |
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| 主要な著者: | , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group UK
2021
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC8131754/ https://ncbi.nlm.nih.gov/pubmed/34006920 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-021-89785-1 |
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