Skip to main content
. 2010 Mar;2(3):a000158. doi: 10.1101/cshperspect.a000158

Figure 2.

Figure 2.

The NEMO molecule. Human NEMO is a 419–amino-acid dimeric molecule essentially structured under the form of a series of parallel intermolecular coiled coils (based on the available structural data). CC1, coiled coil 1; CC2, coiled coil 2; NOA, ubiquitin binding domain; ZF, Zinc Finger (and a second ubiquitin binding domain). The determination of the structure of linker 1 indicated that it is also structured as an intermolecular coiled coil. The structure of CC1 and linker II has not been determined yet. It must be stressed that the dimeric structure of NEMO is relatively unstable in the absence of interacting partners (kinases, polyubiquitin, …). The region of interaction with some of these partners has been indicated: The amino terminus is involved in the interaction with the two kinases. Linker 1 is involved in the interaction with viral transactivators such as HTLV1 Tax and KSHV v-FLIP. The entire carboxy-terminal region is required for transmission of the signal, and the NOA and the ZF domains bind polyubiquitin chains.