Cargando…
Conformational changes in protein kinase A along its activation cycle are rooted in the folding energetics of cyclic-nucleotide binding domains
Cyclic-nucleotide binding (CNB) domains are structurally and evolutionarily conserved signaling modules that regulate proteins with diverse folds and functions. Despite a wealth of structural information, the mechanisms by which CNB domains couple cyclic-nucleotide binding to conformational changes...
Autores principales: | Chau, Amy K., Bracken, Katherine, Bai, Lihui, Pham, Dominic, Good, Lydia L., Maillard, Rodrigo A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10279917/ https://www.ncbi.nlm.nih.gov/pubmed/37150322 http://dx.doi.org/10.1016/j.jbc.2023.104790 |
Ejemplares similares
-
Effects of Ultraviolet Modification on the Gating Energetics of Cyclic Nucleotide–Gated Channels
por: Middendorf, Thomas R., et al.
Publicado: (2000) -
Structure and Energetics of Allosteric Regulation of HCN2 Ion Channels by Cyclic Nucleotides
por: DeBerg, Hannah A., et al.
Publicado: (2016) -
Computational and NMR spectroscopy insights into the conformation of cyclic di-nucleotides
por: Wang, Baifan, et al.
Publicado: (2017) -
Tetracaine Reports a Conformational Change in the Pore of Cyclic Nucleotide–gated Channels
por: Fodor, Anthony A., et al.
Publicado: (1997) -
Conformational Flip of Nonactivated HCN2 Channel Subunits Evoked by Cyclic Nucleotides
por: Thon, Susanne, et al.
Publicado: (2015)