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PDBsum entry 3hs0
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Immune system
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PDB id
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3hs0
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Contents |
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613 a.a.
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233 a.a.
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359 a.a.
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699 a.a.
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References listed in PDB file
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Key reference
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Title
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Insights into complement convertase formation based on the structure of the factor b-Cobra venom factor complex.
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Authors
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B.J.Janssen,
L.Gomes,
R.I.Koning,
D.I.Svergun,
A.J.Koster,
D.C.Fritzinger,
C.W.Vogel,
P.Gros.
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Ref.
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Embo J, 2009,
28,
2469-2478.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Immune protection by the complement system critically depends on assembly of C3
convertases on the surface of pathogens and altered host cells. These
short-lived protease complexes are formed through pro-convertases, which for the
alternative pathway consist of the complement component C3b and the pro-enzyme
factor B (FB). Here, we present the crystal structure at 2.2-A resolution,
small-angle X-ray scattering and electron microscopy (EM) data of the
pro-convertase formed by human FB and cobra venom factor (CVF), a potent
homologue of C3b that generates more stable convertases. FB is loaded onto CVF
through its pro-peptide Ba segment by specific contacts, which explain the
specificity for the homologous C3b over the native C3 and inactive products iC3b
and C3c. The protease segment Bb binds the carboxy terminus of CVF through the
metal-ion dependent adhesion site of the Von Willebrand factor A-type domain. A
possible dynamic equilibrium between a 'loading' and 'activation' state of the
pro-convertase may explain the observed difference between the crystal structure
of CVFB and the EM structure of C3bB. These insights into formation of
convertases provide a basis for further development of complement therapeutics.
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