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Literature summary for 2.3.2.27 extracted from

  • Behera, A.P.; Naskar, P.; Agarwal, S.; Banka, P.A.; Poddar, A.; Datta, A.B.
    Structural insights into the nanomolar affinity of RING E3 ligase ZNRF1 for Ube2N and its functional implications (2018), Biochem. J., 475, 1569-1582 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of ZNRF1 C-terminal domain in complex with Ube2N. The domain binds Ube2N exclusively via its RING domain. The ZNRF1:Ube2N interface contains three salt-bridges/H-bonds involving Glu183 of ZNRF1 and Arg14/Lys10 of Ube2N Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8ND25
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Synonyms

Synonyms Comment Organism
ZNRF1
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Homo sapiens

General Information

General Information Comment Organism
physiological function the RING domain of E3 ligase ZNRF1 binds Ube2N with a Kd of about 50 nM. ZNRF1 interacts with Ube2D2 with a Kd of about 1 mM. The ubiquitination efficiency of ZNRF1:E2 pairs correlates with their affinity. An excess of ZNRF1 inhibits Ube2N-mediated ubiquitination at concentrations at or above 500 nM instead of showing enhanced ubiquitination Homo sapiens