0542005 - BFÚ 2022 RIV NL eng J - Journal Article
Pokorná, Pavlína - Krepl, Miroslav - Šponer, Jiří
Residues flanking the ARK(me3)T/S motif allow binding of diverse targets to the HP1 chromodomain: Insights from molecular dynamics simulations.
Biochimica et Biophysica Acta-General Subjects. Roč. 1865, č. 1 (2021), č. článku 129771. ISSN 0304-4165. E-ISSN 1872-8006
R&D Projects: GA ČR(CZ) GA18-07384S
Institutional support: RVO:68081707
Keywords : heterochromatin protein-1 hp1 * force-field parameters * histone h3 * lysine 9 * secondary structure * structural basis
OECD category: Biochemistry and molecular biology
Impact factor: 4.117, year: 2021 ; AIS: 0.812, rok: 2021
Method of publishing: Limited access
Result website:
https://www.sciencedirect.com/science/article/pii/S0304416520302828?via%3DihubDOI: https://doi.org/10.1016/j.bbagen.2020.129771

Background: The chromodomain (CD) of HP1 proteins is an established H3K9(me3) reader that also binds H1, EHMT2 and H3K23 lysine-methylated targets. Structural experiments have provided atomistic pictures of its recognition of the conserved ARK(me3)S/T motif, but structural dynamics' contribution to the recognition may have been masked by ensemble averaging.
Permanent Link: http://hdl.handle.net/11104/0319504