6y1j

From Proteopedia

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

PDB ID 6y1j

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Structural highlights

6y1j is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.127Å
Ligands:	, , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

1433S_HUMAN Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity). p53-regulated inhibitor of G2/M progression.

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.

References

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