Cargando…
Role of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1
PUMA, which belongs to the BH3-only protein family, is an intrinsically disordered protein (IDP). It binds to its cellular partner Mcl-1 through its BH3 motif, which folds upon binding into an α helix. We have applied a structure-based coarse-grained model, with an explicit Debye—Hückel charge model...
Autores principales: | Chu, Wen-Ting, Clarke, Jane, Shammas, Sarah L., Wang, Jin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5400261/ https://www.ncbi.nlm.nih.gov/pubmed/28369057 http://dx.doi.org/10.1371/journal.pcbi.1005468 |
Ejemplares similares
-
Coupled
Folding and Binding of the Disordered Protein
PUMA Does Not Require Particular Residual Structure
por: Rogers, Joseph M., et al.
Publicado: (2014) -
Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies
por: Shammas, Sarah L., et al.
Publicado: (2016) -
Remarkably Fast Coupled Folding and Binding of the
Intrinsically Disordered Transactivation Domain of cMyb to CBP KIX
por: Shammas, Sarah L., et al.
Publicado: (2013) -
Targeting the apoptotic Mcl-1-PUMA interface with a dual-acting compound
por: Liu, Jiyuan, et al.
Publicado: (2017) -
Diffusion-limited association of disordered protein by non-native electrostatic interactions
por: Kim, Jae-Yeol, et al.
Publicado: (2018)