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.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2005,
437,
505-511)
copyright 2005.
'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 
,
green; MG6^ 
,
pink. e, Intertwined CUB. CUB^g, cyan; CUB^f, red.
Fibronectin-type 3 and CUB strand numbering are indicated.