Backbone resonance assignments of the dimeric domain of the p50 NF-kappaB subunit

Kumar, M and Dadhwal, P and Atreya, HS and Mukherjee, SP (2020) Backbone resonance assignments of the dimeric domain of the p50 NF-kappaB subunit. In: Biomolecular NMR Assignments, 14 (1). pp. 9-11.

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Abstract

The Nuclear Factor kappa-light-chain-enhancer of activated B cells (NF-kappaB) is a family of transcription factor recognizing a 9–11 base pair kappaB sites on the promoter/enhancer region of their target genes. The family comprises of five members forming dimers amongst themselves in various combinations. Here we report the backbone resonance assignments of the 24 kDa homodimer of the p50 subunit of NF-kappaB. This is the first step towards understanding the mechanism of dimer formation in solution. The secondary structure derived from the chemical shifts for the dimer is largely consistent with that observed in the available crystal structures of the protein in DNA-bound form

Item Type:	Journal Article
Publication:	Biomolecular NMR Assignments
Publisher:	Springer
Additional Information:	The copyright for this article belongs to the Springer.
Keywords:	immunoglobulin enhancer binding protein, animal; chemistry; mouse; nuclear magnetic resonance; protein domain; protein multimerization; protein secondary structure, Animals; Mice; NF-kappa B p50 Subunit; Nuclear Magnetic Resonance, Biomolecular; Protein Domains; Protein Multimerization; Protein Structure, Secondary
Department/Centre:	Division of Chemical Sciences > NMR Research Centre (Formerly Sophisticated Instruments Facility)
Date Deposited:	01 Feb 2023 09:12
Last Modified:	01 Feb 2023 09:12
URI:	https://eprints.iisc.ac.in/id/eprint/79677

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