3JSV

Crystal structure of mouse NEMO CoZi in complex with Lys63-linked di-ubiquitin

Summary for 3JSV

• Entry DOI: 10.2210/pdb3jsv/pdb
• Related: 2ZVN 2ZVO 3F89 3FX0
• Descriptor: Ubiquitin, NF-kappa-B essential modulator, ... (4 entities in total)
• Functional Keywords: ubiquitin, coiled-coil, cellular signaling, cytoplasm, isopeptide bond, nucleus, phosphoprotein, ubl conjugation, coiled coil, disulfide bond, metal-binding, transcription, transcription regulation, zinc, zinc-finger, signaling protein-transcription complex, signaling protein/transcription
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (By similarity): O88522
• Total number of polymer chains: 4
• Total formula weight: 39508.04

Authors

Yoshikawa, A.,Sato, Y.,Mimura, H.,Yamashita, M.,Yamagata, A.,Fukai, S. (deposition date: 2009-09-11, release date: 2009-10-27, Last modification date: 2024-10-30)

Primary citation

Yoshikawa, A.,Sato, Y.,Yamashita, M.,Mimura, H.,Yamagata, A.,Fukai, S.
Crystal structure of the NEMO ubiquitin-binding domain in complex with Lys 63-linked di-ubiquitin
Febs Lett., 583:3317-3322, 2009

PubMed Abstract: NEMO is essential for activation of the NF-kappaB signaling pathway, which is regulated by ubiquitination of proteins. The C-terminal leucine zipper of NEMO and its adjacent coiled-coil region (CC2-LZ) reportedly bind to linear ubiquitin chains with 1 microM affinity and to Lys 63-linked chains with 100 microM affinity. Here we report the crystal structure of the CC2-LZ region of mouse NEMO in complex with Lys 63-linked di-ubiquitin (K63-Ub(2)) at 2.7A resolution. The ubiquitin-binding region consists of a 130A-long helix and forms a parallel coiled-coil dimer. The Ile 44-centered hydrophobic patch of ubiquitin is recognized in the middle of the NEMO ubiquitin-binding region. NEMO interacts with each K63-Ub(2)via a single ubiquitin-binding site, consistent with low affinity binding with K63-Ub(2).

PubMed: 19766637
DOI: 10.1016/j.febslet.2009.09.028

Experimental method

X-RAY DIFFRACTION (2.7 Å)