Eoin N. Leen

The paper identifies the DNA binding domain of TFIIIC5 as a key interaction site for N-myc and elucidates the molecular mechanism of their interaction using structural and biophysical methods.

This study uses NMR to analyze the structure, dynamics, and interactions of N-myc's transactivation domain, revealing phosphorylation sites and binding interactions.

The paper shows that TFIIIC binds MYCN and limits non-phosphorylated RNA Polymerase II accumulation at promoters, but does not affect MYCN-dependent gene expression or transcription elongation.