Transient conformations in the unliganded FK506 binding domain of FKBP51 correspond to two distinct inhibitor-bound states

Members of the FK506-binding protein (FKBP) family regulate a range of important physiological processes. Unfortunately, current therapeutics such as FK506 and rapamycin exhibit only modest selectivity among these functionally distinct proteins. Recent progress in developing selective inhibitors has...

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Detalles Bibliográficos
Autores principales: Anderson, Janet S., LeMaster, David M., Hernández, Griselda
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2023
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10514456/
https://www.ncbi.nlm.nih.gov/pubmed/37579948
http://dx.doi.org/10.1016/j.jbc.2023.105159

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10514456/
https://www.ncbi.nlm.nih.gov/pubmed/37579948
http://dx.doi.org/10.1016/j.jbc.2023.105159

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