Cargando…
Phosphorylation of an intrinsically disordered region of Ets1 shifts a multi-modal interaction ensemble to an auto-inhibitory state
Multi-modal interactions are frequently observed in intrinsically disordered regions (IDRs) of proteins upon binding to their partners. In many cases, post-translational modifications in IDRs are accompanied by coupled folding and binding. From both molecular simulations and biochemical experiments...
Autores principales: | Kasahara, Kota, Shiina, Masaaki, Higo, Junichi, Ogata, Kazuhiro, Nakamura, Haruki |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5861456/ https://www.ncbi.nlm.nih.gov/pubmed/29309620 http://dx.doi.org/10.1093/nar/gkx1297 |
Ejemplares similares
-
Molecular mechanisms of cooperative binding of transcription factors Runx1–CBFβ–Ets1 on the TCRα gene enhancer
por: Kasahara, Kota, et al.
Publicado: (2017) -
Molecular Mechanisms of Functional Modulation of Transcriptional
Coactivator PC4 via Phosphorylation on Its Intrinsically Disordered
Region
por: Xie, Qilin, et al.
Publicado: (2023) -
Computer simulation of molecular recognition in biomolecular system: from in silico screening to generalized ensembles
por: Fukunishi, Yoshifumi, et al.
Publicado: (2022) -
Conformational Ensembles of an Intrinsically Disordered Protein pKID with and without a KIX Domain in Explicit Solvent Investigated by All-Atom Multicanonical Molecular Dynamics
por: Umezawa, Koji, et al.
Publicado: (2012) -
Studies on Molecular Dynamics of Intrinsically Disordered Proteins and Their Fuzzy Complexes: A Mini-Review
por: Kasahara, Kota, et al.
Publicado: (2019)