NEMO binding domain of IKK-2 encompasses amino acids 735-745.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Strnad, J; McDonnell, PA; Riexinger, DJ; Mapelli, C; Cheng, L; Gray, H; Ryseck, RP; Burke, JR

Published Date

  • May 2006

Published In

Volume / Issue

  • 19 / 3

Start / End Page

  • 227 - 233

PubMed ID

  • 16583354

Pubmed Central ID

  • 16583354

International Standard Serial Number (ISSN)

  • 0952-3499

Digital Object Identifier (DOI)

  • 10.1002/jmr.766

Language

  • eng

Conference Location

  • England