RelA-Containing NFκB Dimers Have Strikingly Different DNA-Binding Cavities in the Absence of DNA.

ABSTRACT: The main nuclear factor kappa B transcription factor family members RelA-p50 heterodimer and RelA homodimer have different biological functions and show different transcriptional activation profiles. To investigate whether the two family members adopt a similar conformation in their free states, we performed hydrogen-deuterium exchange mass spectrometry, all-atom molecular dynamics simulations, and stopped-flow binding kinetics experiments. Surprisingly, the N-terminal DNA-binding domains adopt an open conformation in RelA-p50 but a closed conformation in RelA homodimer. Both hydrogen-deuterium exchange mass spectrometry and molecular dynamics simulations indicate the formation of an interface between the N-terminal DNA-binding domains only in the RelA homodimer. Such an interface would be

SUBMITTER: Narang D 

PROVIDER: S-EPMC5951767 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature