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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Detalles Bibliográficos
Autores principales: Kriegel, Mark, Wiederanders, Hanna J., Alkhashrom, Sewar, Eichler, Jutta, Muller, Yves A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8131754/
https://www.ncbi.nlm.nih.gov/pubmed/34006920
http://dx.doi.org/10.1038/s41598-021-89785-1

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8131754/
https://www.ncbi.nlm.nih.gov/pubmed/34006920
http://dx.doi.org/10.1038/s41598-021-89785-1

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