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© Research
Publication : BMC structural biology

re-TAMD: exploring interactions between H3 peptide and YEATS domain using enhanced sampling

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in BMC structural biology - 03 Apr 2018

Lamothe G, Malliavin TE

Link to Pubmed [PMID] – 29615024

BMC Struct. Biol. 2018 04;18(1):4

BACKGROUND: Analysis of preferred binding regions of a ligand on a protein is important for detecting cryptic binding pockets and improving the ligand selectivity.

RESULT: The enhanced sampling approach TAMD has been adapted to allow a ligand to unbind from its native binding site and explore the protein surface. This so-called re-TAMD procedure was then used to explore the interaction between the N terminal peptide of histone H3 and the YEATS domain. Depending on the length of the peptide, several regions of the protein surface were explored. The peptide conformations sampled during the re-TAMD correspond to peptide free diffusion around the protein surface.

CONCLUSIONS: The re-TAMD approach permitted to get information on the relative influence of different regions of the N terminal peptide of H3 on the interaction between H3 and YEATS.

https://www.ncbi.nlm.nih.gov/pubmed/29615024