Cargando…
A dynamically coupled allosteric network underlies binding cooperativity in Src kinase
Protein tyrosine kinases are attractive drug targets because many human diseases are associated with the deregulation of kinase activity. However, how the catalytic kinase domain integrates different signals and switches from an active to an inactive conformation remains incompletely understood. Her...
Autores principales: | Foda, Zachariah H., Shan, Yibing, Kim, Eric T., Shaw, David E., Seeliger, Markus A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4300553/ https://www.ncbi.nlm.nih.gov/pubmed/25600932 http://dx.doi.org/10.1038/ncomms6939 |
Ejemplares similares
-
Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites
por: Tong, Michael, et al.
Publicado: (2017) -
An Allosteric Cross-Talk Between the Activation Loop and the ATP Binding Site Regulates the Activation of Src Kinase
por: Pucheta-Martínez, Encarna, et al.
Publicado: (2016) -
Allosteric activation of proto-oncogene kinase Src by GPCR–beta-arrestin complexes
por: Pakharukova, Natalia, et al.
Publicado: (2021) -
Membrane Interaction of Bound Ligands Contributes to the Negative Binding Cooperativity of the EGF Receptor
por: Arkhipov, Anton, et al.
Publicado: (2014) -
Discovery of Non-peptide Small Molecule Allosteric Modulators of the Src-family Kinase, Hck
por: Dorman, Heather R., et al.
Publicado: (2019)