NEMO binding domain of IKK-2 encompasses amino acids 735-745.
NF-kappaB activation is mediated by the IKK signalsome. Though this signalsome is comprised of IKK-1, IKK-2, and NEMO/IKKgamma, it is the interaction between IKK-2 and NEMO that is critical to formation of a functional signalsome. More specifically, previous reports have indicated that this interaction involves the C-terminal LDWSWL residues of ... IKK-2 (called the Nemo Binding Domain (NBD)) and the N-terminus of NEMO. In an effort to characterize the IKK-2:NEMO interaction, we have investigated several NBD-containing peptides for their ability to bind NEMO and inhibit the critical IKK-2:NEMO interaction. The six residue NBD peptide, LDWSWL, showed modest binding to NEMO and little inhibition of the IKK-2:NEMO interaction, whereas peptides containing the NBD plus additional flanking amino acids (NBD-containing peptides) more effectively bound NEMO and inhibited the interaction. These longer NBD-containing peptides may be required to give the NBD an appropriate conformation for recognition by NEMO and/or to provide for additional interactions with NEMO.
Mesh Terms:
Amino Acid Sequence, Amino Acids, Animals, Blotting, Western, Cell Line, Genetic Vectors, Humans, I-kappa B Kinase, Magnetic Resonance Spectroscopy, NF-kappa B, Peptide Fragments, Protein Binding, Protein-Serine-Threonine Kinases, Spodoptera
Amino Acid Sequence, Amino Acids, Animals, Blotting, Western, Cell Line, Genetic Vectors, Humans, I-kappa B Kinase, Magnetic Resonance Spectroscopy, NF-kappa B, Peptide Fragments, Protein Binding, Protein-Serine-Threonine Kinases, Spodoptera
J. Mol. Recognit.
Date: Apr. 04, 2006
PubMed ID: 16583354
View in: Pubmed Google Scholar
Download Curated Data For This Publication
143097
Switch View:
- Interactions 3