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PDBsum entry 3cu7
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Immune system
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PDB id
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3cu7
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References listed in PDB file
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Key reference
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Title
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Structure of and influence of a tick complement inhibitor on human complement component 5.
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Authors
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F.Fredslund,
N.S.Laursen,
P.Roversi,
L.Jenner,
C.L.Oliveira,
J.S.Pedersen,
M.A.Nunn,
S.M.Lea,
R.Discipio,
L.Sottrup-Jensen,
G.R.Andersen.
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Ref.
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Nat Immunol, 2008,
9,
753-760.
[DOI no: ]
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PubMed id
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Abstract
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To provide insight into the structural and functional properties of human
complement component 5 (C5), we determined its crystal structure at a resolution
of 3.1 A. The core of C5 adopted a structure resembling that of C3, with the
domain arrangement at the position corresponding to the C3 thioester being very
well conserved. However, in contrast to C3, the convertase cleavage site in C5
was ordered and the C345C domain flexibly attached to the core of C5. Binding of
the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global
conformation of C5 but did not block the convertase cleavage site. The structure
of C5 may render possible a structure-based approach for the design of new
selective complement inhibitors.
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Figure 2.
(a) Packing of the MG8 (green) and the C5d (gray) domains in
C5 around Ser1007 and Ala1010. (b) The region in a at the
thioester (TE) formed by Cys1009 and Gln1012 in bovine C3
(orange) superimposed onto the C5d domain of C5 (green and gray,
as in a). (c) The thioester formed by Cys838 and Gln841 in TEP
(light blue) and in C5 (green and gray). In b and c, the
catalytic histidine residues 1125 and 951 are in the foreground.
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The above figure is
reprinted
by permission from Macmillan Publishers Ltd:
Nat Immunol
(2008,
9,
753-760)
copyright 2008.
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