3.4.21.43: classical-complement-pathway C3/C5 convertase

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For detailed information about classical-complement-pathway C3/C5 convertase, go to the full flat file.

Reaction

Selective cleavage of Arg-/-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-/- bond in complement component C5 alpha-chain to form C5a and C5b =

Synonyms

C3 convertase, C3/C5 convertase, C3b 2 Bb, C3b2Bb, C3bBb, C3bBbP, C4, C423, C4b,2a, C4b,2a,3b, C4b,C2a, C4b2a, C4b2a(C3b)n, C4b2a3b, C4b2aC3b, C4bC2a, C5 convertase, classical C3 convertase, classical C5 convertase, classical pathway C3 convertase, classical pathway C3/C5 convertase, classical pathway C5 convertase, complement C3 convertase, CP C3 convertase, CP C3/C5 convertase, CP C5 convertase, EAC1,C4b,C2a, EC 3.4.21.44, high affinity C5 convertase, soluble C3 convertase, surface-bound C3 convertase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.43 classical-complement-pathway C3/C5 convertase

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Crystallization

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Crystallization on EC 3.4.21.43 - classical-complement-pathway C3/C5 convertase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structures of the C3b homologue cobra venom factor CVF in complex with C5, and in complex with C5 and the inhibitor SSL7, both at 4.3 A resolution. The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage. CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb

Homo sapiens

P01031

717540

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

-

683775

N-terminal segment C2b, by the hanging-drop vapor-diffusion method, to 1.8 A resolution. Space group P31 with unit-cell parameters a=b= 60.09 A and c = 61.69 A. Conformational changes of C2, C2a and C2b during C3 convertase C4bC2a formation

Homo sapiens

-

695326