Cargando…
A dynamic hydrophobic core orchestrates allostery in protein kinases
Eukaryotic protein kinases (EPKs) constitute a class of allosteric switches that mediate a myriad of signaling events. It has been postulated that EPKs’ active and inactive states depend on the structural architecture of their hydrophobic cores, organized around two highly conserved spines: C-spine...
Autores principales: | Kim, Jonggul, Ahuja, Lalima G., Chao, Fa-An, Xia, Youlin, McClendon, Christopher L., Kornev, Alexandr P., Taylor, Susan S., Veglia, Gianluigi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5384802/ https://www.ncbi.nlm.nih.gov/pubmed/28435869 http://dx.doi.org/10.1126/sciadv.1600663 |
Ejemplares similares
-
Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
por: Wang, Yingjie, et al.
Publicado: (2019) -
Allostery through the computational microscope: cAMP activation of a canonical signaling domain
por: Malmstrom, Robert D., et al.
Publicado: (2015) -
Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases
por: Meharena, Hiruy S., et al.
Publicado: (2016) -
Mapping the Hydrogen Bond Networks in the Catalytic
Subunit of Protein Kinase A Using H/D Fractionation Factors
por: Li, Geoffrey C., et al.
Publicado: (2015) -
Protein Kinase Structure and Dynamics: Role of the αC-β4 Loop
por: Wu, Jian, et al.
Publicado: (2023)