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Literature summary for 3.4.21.43 extracted from

  • Krych-Goldberg, M.; Hauhart, R.E.; Porzukowiak, T.; Atkinson, J.P.
    Synergy between two active sites of human complement receptor type 1 (CD35) in complement regulation: implications for the structure of the classical pathway C3 convertase and generation of more potent inhibitors (2005), J. Immunol., 175, 4528-4535.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N-terminal long homologous repeat A of complement receptor type 1 responsible for dissociation of enzyme. Highest decay accelerating activity for mutant dimeric construct N-terminal long homologous repeat A (D109N/E116K)/N-terminal long homologous repeat A (D109N) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Subunits

Subunits Comment Organism
dimer dimeric structure of enzyme on cell surfaces, binding studies Homo sapiens
More enzyme subunit C3b binds to site 2 of complement receptor type 1 Homo sapiens