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Hidden dynamic signatures drive substrate selectivity in the disordered phosphoproteome
Phosphorylation sites are hyperabundant in the eukaryotic disordered proteome, suggesting that conformational fluctuations play a major role in determining to what extent a kinase interacts with a particular substrate. In biophysical terms, substrate selectivity may be determined not just by the str...
| Autores principales: | , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
National Academy of Sciences
2020
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7519349/ https://www.ncbi.nlm.nih.gov/pubmed/32900925 http://dx.doi.org/10.1073/pnas.1921473117 |