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Literature summary for 2.3.2.31 extracted from

  • Kumar, A.; Chaugule, V.K.; Condos, T.E.C.; Barber, K.R.; Johnson, C.; Toth, R.; Sundaramoorthy, R.; Knebel, A.; Shaw, G.S.; Walden, H.
    Parkin-phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity (2017), Nat. Struct. Mol. Biol., 24, 475-483 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
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 Homo sapiens

Protein Variants

Protein Variants Comment Organism
C431S/H433A RING2 mutant, able to trap the catalytic parkin-ubiquitin intermediate Homo sapiens
E321A/C431S/H433A UBR2 patch mutant of parkin. In contrast to C431S/H433A, this mutant is defective in ubiquitin charging even in the presence of phosphoubiquitin Homo sapiens
H302A/E321A/C431S/H433A 60fold reduced in ubiquitin charging of the RING2 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O60260
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General Information

General Information Comment Organism
physiological function the activity of inactive parkin molecules can be stimulated by the presence of activated parkin molecules, molecules can function together to ligate ubiquitin Homo sapiens