Characterization of the dynamics and the conformational entropy in the binding between TAZ1 and CTAD-HIF-1α.

ABSTRACT: The interaction between the C-terminal transactivation domain of HIF-1α (CTAD-HIF-1α) and the transcriptional adapter zinc binding 1 (TAZ1) domain of CREB binding protein participate in the initiation of gene transcription during hypoxia. Unbound CTAD-HIF-1α is disordered but undergoes a disorder-to-order transition upon binding to TAZ1. We have here performed NMR side chain and backbone relaxation studies on TAZ1 and side chain relaxation measurements on CTAD-HIF-1α in order to investigate the role of picosecond to nanosecond dynamics. We find that the internal motions are significantly affected upon binding, both on the side chain and the backbone level. The dynamic response corresponds to a conformational entropy change that contributes substantially to the binding thermodynamics for bo

SUBMITTER: Nyqvist I 

PROVIDER: S-EPMC6851107 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature