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Publication Abstract from PubMed

Inflammatory responses mediated by the transcription factor nuclear factor kappa-light-chain enhancer of activated B cells (NF-kappaB) play key roles in immunity, autoimmune diseases, and cancer. NF-kappaB is directly regulated through protein-protein interactions, including those with IkappaB and 14-3-3 proteins. These two important regulatory proteins have been reported to interact with each other, although little is known about this interaction. We analyzed the inhibitor of nuclear factor kappa B alpha (IkappaBalpha)/14-3-3sigma interaction via a peptide/protein-based approach. Structural data were acquired via X-ray crystallography, while binding affinities were measured with fluorescence polarization assays and time-resolved tryptophan fluorescence. A high-resolution crystal structure (1.13 A) of the uncommon 14-3-3 interaction motif of IkappaBalpha (IkappaBalphapS63) in a complex with 14-3-3sigma was evaluated. This motif harbors a tryptophan that makes this crystal structure the first one with such a residue visible in the electron density at that position. We used this tryptophan to determine the binding affinity of the unlabeled IkappaBalpha peptide to 14-3-3 via tryptophan fluorescence decay measurements.

Interaction of an IkappaBalpha Peptide with 14-3-3.,Wolter M, Santo DL, Herman P, Ballone A, Centorrino F, Obsil T, Ottmann C ACS Omega. 2020 Mar 6;5(10):5380-5388. doi: 10.1021/acsomega.9b04413. eCollection, 2020 Mar 17. PMID:32201828^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.