. Author manuscript; available in PMC: 2013 Nov 5.

Published in final edited form as: Immunol Lett. 2004 Sep;95(2):10.1016/j.imlet.2004.06.015. doi: 10.1016/j.imlet.2004.06.015

Table 3.

Most variable residues within gC1q identified by ConSurf

	ghA		ghB		ghC
1	● PRO²	102	●ASN²	104	● HIS ²	101
2	● MET¹	104	● PRO ²	106	● PRO ²	103
3	●GLY²	105	● ARG ¹	108	● ALA ¹	105
4	ILE ¹	110	● ARG ¹	109	● PRO ¹	106
5	○GLN¹	118	ARG ¹ ★	114	●SER²	108
6	○GLU²	120	MET ¹	122	● ARG ¹	111
7	HIS ²	125	ARG ² ★	129	○ PRO ¹	119
8	THR¹	132	LYS ²	136	○GLY²	121
9	GLN¹	146	ARG ¹	150	SER²	126
10	SER²	152	●GLU¹★	162	LYS ¹	133
11	● ARG ¹	158	● ALA ¹	164	THR¹	147
12	● VAL ¹	161	● LYS ²	166	LEU ²	153
13	● ARG ¹	163	CYS ²	171	VAL ¹	159
14	CYS ¹	168	● TYR ¹ ◀	175	● CYS ¹	165
15	ASN¹	172	●PHE²	178	●SER¹	169
16	●GLN²	186	○ LYS ²	188	●ASN²	172
17	●GLN¹	188	○GLU¹	190	○ ARG ¹	182
18	●GLN¹	189	○GLN¹	191	○GLN¹	184
19	○ PRO ¹	199	●ASP¹	201	○ VAL ¹	185
20	○ LYS ¹ ◀	200	● LYS ¹	202	●ASP¹	195
21	○ HIS ¹	203	○ MET ¹	208	● TYR ¹	196
22	SER¹	208	○GLU²	209	○GLY²	201
23			○GLY¹	210	○ ILE ¹	202
24					○GLN²	203
25					○GLY¹	204

(★) Residues known to be involved in IgG binding; (◀) residues proposed to be involved in CRP binding. Residues are sorted on the basis of position. (●) and (○) indicate possible important residue clusters for ligand binding. Clusters are defined wherever residues are at/within 3-residue distance from each other. Hydrophobic and ring residues are underlined. Arginine and lysine residues are shown in boldface. Numbers in superscript indicate the “rank” of the residue given by ConSurf (1–9, most variable to most conserved, see also Fig. 2). The most variable residues (ranks 1 and 2) are shown here. Only the gC1q domain was used in the analysis.