Backbone H, C, and N NMR resonance assignments of the Krüppel-like factor 4 activation domain.

Krüppel-like factor 4 (KLF4) is a transcription factor involved in diverse biological processes, including development, cellular differentiation and proliferation, and maintenance of tissue homeostasis. KLF4 has also been associated with disease states, such as cardiovascular disease and several cancers. KLF4 contains an activation domain, repression domain, and a structurally characterized C-terminal zinc finger domain that mediates its binding to DNA. The structurally uncharacterized KLF4 activation domain is critical for transactivation by KLF4 and mediates its binding to the transcriptional coactivator CBP/p300. Here, we report the H, N, CO, Cα and Cβ NMR chemical shift assignments of KLF4, which contains the KLF4 activation domain. Narrow chemical shift dispersion in the H dimension of the H-N HSQC spectrum suggests that the KLF4 fragment is intrinsically disordered.