Residues flanking the ARK
| Autor: | Pavlína, Pokorná, Miroslav, Krepl, Jiří, Šponer |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Histones
Chromobox Protein Homolog 5 Chromosomal Proteins Non-Histone Histocompatibility Antigens Lysine Humans Protein Interaction Domains and Motifs Amino Acid Sequence Histone-Lysine N-Methyltransferase Molecular Dynamics Simulation Methylation Protein Processing Post-Translational Protein Binding |
| Zdroj: | Biochimica et biophysica acta. General subjects. 1865(1) |
| ISSN: | 1872-8006 |
| Popis: | The chromodomain (CD) of HP1 proteins is an established H3K9We acquired ~350 μs of explicit solvent molecular dynamics (MD) simulations of the CD domain interacting with several peptides using the latest AMBER force fields.The simulations reproduced the experimentally observed static binding patterns well but also revealed visible structural dynamics at the interfaces. While the buried KThe CD reads a longer target segment than previously thought, ranging from positions -7 to +3. The CD anionic clamp can be neutralized not only by the -3 and -1 residues, but also by -7, -6, -5 and +3 residues.Structural dynamics, not immediately apparent from the structural data, contribute to molecular recognition between the HP1 CD domain and its targets. Mutual replaceability of target residues increases target sequence flexibility. |
| Databáze: | OpenAIRE |
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