Conformational Switching of Human G-Quadruplexed DNA with Ligand Binding under Molecular Crowding Conditions

Abstract

revealed observable and quantifiable conformational changes at the ATP and RNA binding sites. Trajectories of minimum distances among residues, and model-to-model ratios of RMSF were used as parameters to quantify the structural effects of the mutations. Atomic interactions propagated from the mutational residues to both ATP and RNA binding sites were observed due to the changes of side chains of these mutations. We hypothesize these three residues play structural roles in the unique functions of DbpA in rRNA interactions. Future studies targeting key unique residues may reveal connected allosteric pathways within the protein structure and assist studying the diversity of function among DEAD-box proteins.