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Literature summary for 3.4.21.43 extracted from

  • Krishnan, V.; Xu, Y.; Macon, K.; Volanakis, J.E.; Narayana, S.V.
    The crystal structure of C2a, the catalytic fragment of classical pathway C3 and C5 convertase of human complement (2007), J. Mol. Biol., 367, 224-233.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of C2 in insect cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
Mg2+-bound C2a, hanging drop vapor diffusion method, 22°C, 0.002 ml of 20 mg/ml protein solution is mixed with 0.002 ml of well solution containing 20% w/v polyethylene glycol 10000, 0.1 M HEPES, pH 7.5, and 0.0004 ml of 0.3 M glycyl-glycyl-glycine, 3-7 days, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required during enzyme formation Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the multi-domain serine protease C2 is the catalytic fragment of classical pathway C3 and C5 convertase of human complement of the classical and lectin pathways of complement activation, formation of these convertases requires the Mg2+-dependent binding of C2 to C4b and the subsequent cleavage of C2 by C1s or MASP2, respectively, the C-terminal fragment C2a consisting of a serine protease and a von Willebrand factor type A domain, remains attached to C4b, forming the C3 convertase, C4b2a, structure, overview ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein C2 is a glycosylated modular protein consisting of three domains Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the multi-domain serine protease C2 is the catalytic fragment of classical pathway C3 and C5 convertase of human complement of the classical and lectin pathways of complement activation, formation of these convertases requires the Mg2+-dependent binding of C2 to C4b and the subsequent cleavage of C2 by C1s or MASP2, respectively, the C-terminal fragment C2a consisting of a serine protease and a von Willebrand factor type A domain, remains attached to C4b, forming the C3 convertase, C4b2a, structure, overview Homo sapiens ?
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Subunits

Subunits Comment Organism
More C2 is a glycosylated modular protein consisting of three domains, C2a is the catalytic fragment of classical pathway C3 and C5 convertase of human complement, formation of the convertases requires the Mg2+-dependent binding of C2 to C4b and the subsequent cleavage of C2 by C1s or MASP2, respectively, the C-terminal fragment C2a consisting of a serine protease and a von Willebrand factor type A domain, remains attached to C4b, forming the C3 convertase, C4b2a, three-dimensional structure of the C2a molecule, residues Asp240, Ser242, Ser244, Thr317 and Asp356 constitute the MIDAS motif of C2a, overview Homo sapiens

Synonyms

Synonyms Comment Organism
C3 convertase
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Homo sapiens
C3bBb alternative pathway C3 convertase Homo sapiens
C4b2a
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Homo sapiens
C5 convertase
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Homo sapiens