Study reports structural and molecular determinant(s) of target specificity of actin histidine vs. lysine in the active site of SETD3. To facilitate the methyl transfer reaction SETD3 provides a local environment that promotes deprotonation of the target nitrogen N3 of histidine (and concomitant protonation of N1).
Findings indicate that SET domain protein 3 (SETD3) down-regulated the expression of kinesin light chain 4 (KLC4) contributing to the radiosensitivity of cervical cancer cells suggesting targeting SETD3 might be a potential strategy for the clinical management of cervical cancer.
Structural analyses supported by biochemical experiments and enzyme activity assays indicate that the recognition and methylation of beta-actin by SETD3 are highly sequence specific and that both SETD3 and beta-actin adopt pronounced conformational changes upon binding to each other
Low expression of SETD3 is a reliable predictor of poor survival in colorectal cancer patients. SETD3 is a positive regulator of p53-dependent activation of DOX-induced apoptosis.
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