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. 2016 Jan 19;110(2):327–337. doi: 10.1016/j.bpj.2015.12.015

Figure 2.

Figure 2

(a) Distance populations for Lys40 to DNA phosphate show an interaction that is unique to macroH2A-like L1 loops. (b) A representative configuration of the Lys side chain stretching across the molecule to interact with the dimer’s nonassociated DNA. This orientation sterically hinders the symmetric loop from forming a similar interaction. This interaction contributes significantly to stabilizing DNA-octamer binding in the macroH2A and L1-mutant systems. To see this figure in color, go online.