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* Residue conservation analysis
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DOI no:
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Nature
437:505-511
(2005)
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PubMed id:
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Structures of complement component C3 provide insights into the function and evolution of immunity.
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B.J.Janssen,
E.G.Huizinga,
H.C.Raaijmakers,
A.Roos,
M.R.Daha,
K.Nilsson-Ekdahl,
B.Nilsson,
P.Gros.
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ABSTRACT
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The mammalian complement system is a phylogenetically ancient cascade system
that has a major role in innate and adaptive immunity. Activation of component
C3 (1,641 residues) is central to the three complement pathways and results in
inflammation and elimination of self and non-self targets. Here we present
crystal structures of native C3 and its final major proteolytic fragment C3c.
The structures reveal thirteen domains, nine of which were unpredicted, and
suggest that the proteins of the alpha2-macroglobulin family evolved from a core
of eight homologous domains. A double mechanism prevents hydrolysis of the
thioester group, essential for covalent attachment of activated C3 to target
surfaces. Marked conformational changes in the alpha-chain, including movement
of a critical interaction site through a ring formed by the domains of the
beta-chain, indicate an unprecedented, conformation-dependent mechanism of
activation, regulation and biological function of C3.
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Selected figure(s)
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Figure 1.
Figure 1: Structures of human complement components C3 and C3c.
a, b, Ribbon representation of native C3 (13 domains) and C3c
(10 domains), respectively. Also shown are intact thioester (red
spheres), anchor region (grey) and  'NT
(black). c, Domain sequence and arrangements in C3 and C3c. The
colour scheme matches that in a, b. Shown are the thioester site
(white triangle), disulphide bridges, glycan positions (for
details see Supplementary Figs 3 and 6) and cleavage sites.
Sequential proteolysis from C3 to C3c is indicated. d, e,
Intertwined domains. d, MG6 intertwines the  -
and -chain
of mature C3. MG6^  ,
green; MG6^  ,
pink. e, Intertwined CUB. CUB^g, cyan; CUB^f, red.
Fibronectin-type 3 and CUB strand numbering are indicated.
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Figure 5.
Figure 5: The alpha- 'NT
region (residues 727-744) slips through the beta- -ring.
a, Two views, rotated by 180°, of the cone formed by ANA, MG3
and MG8 (surface representation), and residues 730-744 (stick
representation). Residues important for factor B binding are
labelled. b, The 'NT
regions are on opposite sides of the molecule in C3 and C3c. In
C3 this region is covalently linked to ANA; the scissile bond
726-727 is part of a disordered loop 720-729 (dashed line). Also
shown are surface contours of C3 and C3c (transparent light
grey), residues 727-767 (green sticks), ANA and MG6 (ribbons),
and MG2 and MG3 of the -ring
(spheres).
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2005,
437,
505-511)
copyright 2005.
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Figures were
selected
by the author.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.S.Laursen,
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PDB codes:
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PDB code:
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J Biol Chem,
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PDB code:
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K.W.Ferrara,
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Nat Immunol,
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PDB code:
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Structure,
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PDB code:
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Nat Immunol,
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PDB code:
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F.Yoshizaki,
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Biomaterials,
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Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition.
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J Biol Chem,
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PDB code:
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PDB codes:
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(2007).
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J Biol Chem,
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PDB code:
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M.Pasupuleti,
B.Walse,
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J Biol Chem,
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M.van Lookeren Campagne,
C.Wiesmann,
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Macrophage complement receptors and pathogen clearance.
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Cell Microbiol,
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(2007).
The structure of OMCI, a novel lipocalin inhibitor of the complement system.
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J Mol Biol,
369,
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PDB codes:
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R.H.Baxter,
C.I.Chang,
Y.Chelliah,
S.Blandin,
E.A.Levashina,
and
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(2007).
Structural basis for conserved complement factor-like function in the antimalarial protein TEP1.
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| |
Proc Natl Acad Sci U S A,
104,
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PDB code:
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R.P.Rother,
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Discovery and development of the complement inhibitor eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria.
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Nat Biotechnol,
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A derivative of the plasma protease inhibitor alpha(2)-macroglobulin regulates the response to peripheral nerve injury.
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J Neurochem,
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A.Abdul Ajees,
K.Gunasekaran,
J.E.Volanakis,
S.V.Narayana,
G.J.Kotwal,
and
H.M.Murthy
(2006).
The structure of complement C3b provides insights into complement activation and regulation.
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| |
Nature,
444,
221-225.
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PDB code:
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A.P.Herbert,
D.Uhrín,
M.Lyon,
M.K.Pangburn,
and
P.N.Barlow
(2006).
Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure.
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J Biol Chem,
281,
16512-16520.
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PDB code:
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B.J.Janssen,
A.Christodoulidou,
A.McCarthy,
J.D.Lambris,
and
P.Gros
(2006).
Structure of C3b reveals conformational changes that underlie complement activity.
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| |
Nature,
444,
213-216.
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PDB code:
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C.Wiesmann,
K.J.Katschke,
J.Yin,
K.Y.Helmy,
M.Steffek,
W.J.Fairbrother,
S.A.McCallum,
L.Embuscado,
L.DeForge,
P.E.Hass,
and
M.van Lookeren Campagne
(2006).
Structure of C3b in complex with CRIg gives insights into regulation of complement activation.
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| |
Nature,
444,
217-220.
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PDB codes:
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F.J.Milder,
H.C.Raaijmakers,
M.D.Vandeputte,
A.Schouten,
E.G.Huizinga,
R.A.Romijn,
W.Hemrika,
A.Roos,
M.R.Daha,
and
P.Gros
(2006).
Structure of complement component C2A: implications for convertase formation and substrate binding.
|
| |
Structure,
14,
1587-1597.
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PDB codes:
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J.N.Arnold,
R.Wallis,
A.C.Willis,
D.J.Harvey,
L.Royle,
R.A.Dwek,
P.M.Rudd,
and
R.B.Sim
(2006).
Interaction of mannan binding lectin with alpha2 macroglobulin via exposed oligomannose glycans: a conserved feature of the thiol ester protein family?
|
| |
J Biol Chem,
281,
6955-6963.
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L.A.Pirofski
(2006).
Of mice and men, revisited: new insights into an ancient molecule from studies of complement activation by Cryptococcus neoformans.
|
| |
Infect Immun,
74,
3079-3084.
|
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M.Carroll
(2006).
Immunology: exposure of an executioner.
|
| |
Nature,
444,
159-160.
|
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M.Nonaka,
and
A.Kimura
(2006).
Genomic view of the evolution of the complement system.
|
| |
Immunogenetics,
58,
701-713.
|
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N.Nishida,
T.Walz,
and
T.A.Springer
(2006).
Structural transitions of complement component C3 and its activation products.
|
| |
Proc Natl Acad Sci U S A,
103,
19737-19742.
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T.A.Springer
(2006).
Complement and the multifaceted functions of VWA and integrin I domains.
|
| |
Structure,
14,
1611-1616.
|
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T.S.Jokiranta,
V.P.Jaakola,
M.J.Lehtinen,
M.Pärepalo,
S.Meri,
and
A.Goldman
(2006).
Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.
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| |
EMBO J,
25,
1784-1794.
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PDB code:
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T.S.Jokiranta
(2006).
C3b and factor H: key components of the complement system.
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| |
Expert Rev Clin Immunol,
2,
775-786.
|
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R.Liddington,
and
L.Bankston
(2005).
Structural biology: origins of chemical biodefence.
|
| |
Nature,
437,
484-485.
|
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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