4DBG

Crystal structure of HOIL-1L-UBL complexed with a HOIP-UBA derivative

Summary for 4DBG

• Entry DOI: 10.2210/pdb4dbg/pdb
• Descriptor: RanBP-type and C3HC4-type zinc finger-containing protein 1, RING finger protein 31 (3 entities in total)
• Functional Keywords: ubiquitin fold, ubiquitination, ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (By similarity): Q96EP0
• Total number of polymer chains: 2
• Total formula weight: 30227.96

Authors

Yagi, H.,Hiromoto, T.,Mizushima, T.,Kurimoto, E.,Kato, K. (deposition date: 2012-01-15, release date: 2012-04-04, Last modification date: 2024-10-09)

Primary citation

Yagi, H.,Ishimoto, K.,Hiromoto, T.,Fujita, H.,Mizushima, T.,Uekusa, Y.,Yagi-Utsumi, M.,Kurimoto, E.,Noda, M.,Uchiyama, S.,Tokunaga, F.,Iwai, K.,Kato, K.
A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex
Embo Rep., 13:462-468, 2012

PubMed Abstract: HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-κB activation. This study highlights the versatility and specificity of protein-protein interactions involving Ub/UBLs and their cognate proteins.

PubMed: 22430200
DOI: 10.1038/embor.2012.24

Experimental method

X-RAY DIFFRACTION (2.71 Å)