Cargando…
Dynamics and Flexibility of Human Aromatase Probed by FTIR and Time Resolved Fluorescence Spectroscopy
Human aromatase (CYP19A1) is a steroidogenic cytochrome P450 converting androgens into estrogens. No ligand-free crystal structure of the enzyme is available to date. The crystal structure in complex with the substrate androstenedione and the steroidal inhibitor exemestane shows a very compact confo...
Autores principales: | Di Nardo, Giovanna, Breitner, Maximilian, Sadeghi, Sheila J., Castrignanò, Silvia, Mei, Giampiero, Di Venere, Almerinda, Nicolai, Eleonora, Allegra, Paola, Gilardi, Gianfranco |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859599/ https://www.ncbi.nlm.nih.gov/pubmed/24349198 http://dx.doi.org/10.1371/journal.pone.0082118 |
Ejemplares similares
-
Polymorphism on human aromatase affects protein dynamics and substrate binding: spectroscopic evidence
por: Di Nardo, Giovanna, et al.
Publicado: (2021) -
Molecular and Structural Evolution of Cytochrome P450 Aromatase
por: Di Nardo, Giovanna, et al.
Publicado: (2021) -
Depicting the proton relay network in human aromatase: New insights into the role of the alcohol‐acid pair
por: Zhang, Chao, et al.
Publicado: (2022) -
Molecular Lego of Human Cytochrome P450: The Key Role of Heme Domain Flexibility for the Activity of the Chimeric Proteins
por: Catucci, Gianluca, et al.
Publicado: (2022) -
The Odd Faces of Oligomers: The Case of TRAF2-C, A Trimeric C-Terminal Domain of TNF Receptor-Associated Factor
por: Di Venere, Almerinda, et al.
Publicado: (2021)