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Literature summary for 2.3.2.27 extracted from

  • Taherbhoy, A.; Huang, O.; Cochran, A.
    BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase (2015), Nat. Commun., 6, 7621.
    View publication on PubMed
Search for more literature for 2.3.2.27

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with polycomb group RING finger proteins PCGF5 or PCGF4 and E2 enzyme UbcH5. RING1B binds directly to UbcH5c, with the PCGF partner making no contacts with the E2. The catalytically critical hydrogen bond between RING1B R91 and the backbone carbonyl of UbcH5c Q92 is present in both the structures, consistent with an activated conformation of the E2. Differences between the PCGF4 and PCGF5 ternary complex structures are found at the N termini of the PCGF and RING1B Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99496
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information isoform RING1B acts in complex with polycomb group RING finger proteins PCGF. Complexes with PCGF4/BMI1 and PCGF2/Mel-18 support only low-level intrinsic RING1B activity in auto-ubiquitination or E2 discharge assays. A salt-bridge between K73–D77 in RING1B–PCGF4 both interferes sterically with the close approach of ubiquitin and limits the capacity of D77 to engage in alternative interactions. The low activity of the PCGF4–RING1B heterodimer is offset by a relatively favourable interaction with nucleosome substrates, resulting in an efficient site-specific monoubiquitination Homo sapiens ?
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Synonyms

Synonyms Comment Organism
Ring1B
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 Homo sapiens