Cargando…
Loss of stability and unfolding cooperativity in hPGK1 upon gradual structural perturbation of its N-terminal domain hydrophobic core
Phosphoglycerate kinase has been a model for the stability, folding cooperativity and catalysis of a two-domain protein. The human isoform 1 (hPGK1) is associated with cancer development and rare genetic diseases that affect several of its features. To investigate how mutations affect hPGK1 folding...
Autores principales: | Pacheco-García, Juan Luis, Loginov, Dmitry S., Naganathan, Athi N., Vankova, Pavla, Cano-Muñoz, Mario, Man, Petr, Pey, Angel L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9561527/ https://www.ncbi.nlm.nih.gov/pubmed/36229482 http://dx.doi.org/10.1038/s41598-022-22088-1 |
Ejemplares similares
-
Allosteric Communication in the Multifunctional and Redox NQO1 Protein Studied by Cavity-Making Mutations
por: Pacheco-Garcia, Juan Luis, et al.
Publicado: (2022) -
Structural basis of the pleiotropic and specific phenotypic consequences of missense mutations in the multifunctional NAD(P)H:quinone oxidoreductase 1 and their pharmacological rescue
por: Pacheco-Garcia, Juan Luis, et al.
Publicado: (2021) -
pPerturb: A Server for Predicting Long-Distance Energetic
Couplings and Mutation-Induced Stability Changes in Proteins via Perturbations
por: Gopi, Soundhararajan, et al.
Publicado: (2020) -
Protein Stability, Folding and Misfolding in Human PGK1 Deficiency
por: Valentini, Giovanna, et al.
Publicado: (2013) -
A binding cooperativity switch driven by synergistic structural swelling of an osmo-regulatory protein pair
por: Narayan, Abhishek, et al.
Publicado: (2019)