X-ray Crystal Structure of an IκBβ·NF-κB p65 Homodimer Complex*
By S. Malek, De-bin Huang, T. Huxford, S. Ghosh, G. Ghosh. Journal of Biological Chemistry, 2003
115 citations recorded by the source corpus.
We report the crystal structure of a murine IκBβ·NF-κB p65 homodimer complex. Crystallographic models were determined for two triclinic crystalline systems and refined against data at 2.5 and 2.1 Å. The overall complex structure is similar to that of the IκBα·NF-κB p50/p65 heterodimer complex. One NF-κB p65 subunit nuclear localization signal clearly contacts IκBβ, whereas a homologous segment from the second subunit of the homodimer is mostly solvent-exposed. The unique 47-amino acid insertion between ankyrin repeats three and four of IκBβ is mostly disordered in the structure. Primary sequence analysis and differences in the mode of binding at the IκBβ sixth ankyrin repeat and NF-κB p65 homodimer suggest a model for nuclear IκBβ·NF-κB·DNA ternary complex formation. These unique structural features of IκBβ may contribute to its ability to mediate persistent NF-κB activation.
Subfields: Urban Studies
View Paper: https://www.semanticscholar.org/paper/9b244cc5ce795ee9be5c6cd00b1ad9edd0917acf
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Citations in the corpus
- Transcriptional regulation via the NF-κB signaling module (2006, background): “IkBa has a higher affinity for the p50:RelA heterodimer than the RelA homodimer (Malek et al., 2003), and RelB-containing dimers are not bound by the three canonical IkB proteins, but can be bound by the ARD of p100 (Solan et al., 2002; Derudder et al., 2003; Basak et al., 2006).”
- Molecular Basis of NF-κB Signaling (2013, background): “Furthermore, the NEMOZF was shown to be a ubiquitin-binding domain, which binds ubiquitin with a 1:1 stoichiometry and submillimolar affinity (12, 27, 74).”