6Y1J

14-3-3 sigma in complex with IkappaBalpha pS63 peptide

Summary for 6Y1J

• Entry DOI: 10.2210/pdb6y1j/pdb
• Descriptor: 14-3-3 protein sigma, NF-kappa-B inhibitor alpha, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: 14-3-3 sigma, ikba, nf-kb, peptide binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 30687.81

Authors

Wolter, M.,Ottmann, C. (deposition date: 2020-02-12, release date: 2020-03-04, Last modification date: 2024-10-16)

Primary citation

Wolter, M.,Santo, D.L.,Herman, P.,Ballone, A.,Centorrino, F.,Obsil, T.,Ottmann, C.
Interaction of an I kappa B alpha Peptide with 14-3-3.
Acs Omega, 5:5380-5388, 2020

PubMed Abstract: Inflammatory responses mediated by the transcription factor nuclear factor kappa-light-chain enhancer of activated B cells (NF-κB) play key roles in immunity, autoimmune diseases, and cancer. NF-κB is directly regulated through protein-protein interactions, including those with IκB 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 α (IκBα)/14-3-3σ 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 Å) of the uncommon 14-3-3 interaction motif of IκBα (IκBαpS63) in a complex with 14-3-3σ 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 IκBα peptide to 14-3-3 via tryptophan fluorescence decay measurements.

PubMed: 32201828
DOI: 10.1021/acsomega.9b04413

Experimental method

X-RAY DIFFRACTION (1.127 Å)