Towards Unraveling the Histone Code by Fragment Blind Docking.

ABSTRACT: Histones serve as protein spools for winding the DNA in the nucleosome. High variability of their post-translational modifications result in a unique code system often responsible for the pathomechanisms of epigenetics-based diseases. Decoding is performed by reader proteins via complex formation with the N-terminal peptide tails of histones. Determination of structures of histone-reader complexes would be a key to unravel the histone code and the design of new drugs. However, the large number of possible histone complex variations imposes a true challenge for experimental structure determination techniques. Calculation of such complexes is difficult due to considerable size and flexibility of peptides and the shallow binding surfaces of the readers. Moreover, location of the binding sites

SUBMITTER: Balint M 

PROVIDER: S-EPMC6358888 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature