Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.
 

Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.

Related Articles Backbone (1)H, (13)C, and (15)N NMR resonance assignments of the Krüppel-like factor 4 activation domain.

Biomol NMR Assign. 2017 Feb 28;:

Authors: Conroy BS, Weiss ER, Smith SP, Langelaan DN

Abstract
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 (1)H, (15)N, (13)CO, (13)C? and (13)C? NMR chemical shift assignments of KLF41-130, which contains the KLF4 activation domain. Narrow chemical shift dispersion in the (1)H dimension of the (1)H-(15)N HSQC spectrum suggests that the KLF41-130 fragment is intrinsically disordered.


PMID: 28247282 [PubMed - as supplied by publisher]



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