EC Number   |
|---|
   2.3.2.31 | cocrystal structure of HOIP RBR domain with single-domain antibody, use as a platform for soaking of ligands that target the active site cysteine of HOIP |
| 2.3.2.31 | structure of a parkin-phosphoubiquitin complex. Phosphoubiquitin binding induces a movement in the IBR domain to reveal a cryptic ubiquitin binding site. Mutation of this site negatively impacts on Parkin's activity. Ubiquitin binding promotes cooperation between parkin molecules |
| 2.3.2.31 | structure of ARIH1 in complex with UbcH7-ubiquitin, to 3.2 A resolution. ARIH1 is autoinhibited even in the complex. The ARIH1 UBA-L domain binds to ubiquitin and NEDD8 |
| 2.3.2.31 | structure of isoform HHARI, in complex with a UbcH7-ubiquitin thioester mimetic. Mechanistically important conformational changes in the RING1 and UBA-like domains of HHARI accompany UbcH7-ubiquitin binding. HHARI recruits E2-ubiquitin in an open conformation. HHARI optimally functions with UbcH7 that solely performs transthiolation, and HHARI prevents spurious discharge of ubiquitin from E2 to lysine residues by harboring structural elements that block E2-ubiquitin from adopting a closed conformation and participating in contacts to ubiquitin that promote an open E2-ubiquitin conformation |
| 2.3.2.31 | structure of the fully active HOIP-RBR in its transfer complex with an E2-ubiquitin conjugate. HOIP-RBR binds the E2-ubiquitin conjugate in an elongated fashion, with the E2 and E3 catalytic centers aligned for ubiquitin transfer, which structurally both requires and enables a HECT-like mechanism. Three distinct helix-IBR-fold motifs form ubiquitin-binding regions that engage the activated ubiquitin of the E2-ubiquitin conjugate as well as an additional regulatory ubiquitin molecule |
