Deciphering the role of dimer interface in intrinsic dynamics and allosteric pathways underlying the functional transformation of DNMT3A

• Published in: Biochimica et biophysica acta Vol. 1862; no. 7; pp. 1667 - 1679
• Main Authors: Liang, Zhongjie, Hu, Junchi, Yan, Wenying, Jiang, Hualiang, Hu, Guang, Luo, Cheng
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.07.2018
• Subjects: Allosteric communication; Allosteric Regulation; Catalytic Domain; Conformational dynamics; Dimerization; DNA (Cytosine-5-)-Methyltransferases - chemistry; Elastic network models, network theory, coevolution analysis; Histones - metabolism; Humans; Information Theory; Models, Chemical; Models, Molecular; Motion; Protein Binding; Protein Conformation; Protein Domains; Signal Transduction; Structure-Activity Relationship; Elastic network models, network theory, coevolution analysis; Conformational dynamics; Allosteric communication

DNMT3A, as de novo DNA methyltransferase, is essential for regulating gene expression through cellular development and differentiation. The functions of DNMT3A rely on its oligomeric states and allosteric regulations between its catalytic domain and binding partners. Despite recent resolution of aut...