. 2011 Feb 1;108(7):2897–2902. doi: 10.1073/pnas.1017087108

Table 1.

Location and reported functional consequences of surface-exposed aHUS-associated mutations within FH19–20 and C3d part of C3b

		Reported functional defects^*
Location in FH19–20:C3d	Mutations	FH–C3b/d	FH–heparin
aHUS mutations on FH19–20 surface
FH19 site	Asp1119Gly^†	↓	↔
FH19 site	Tyr1142Asp/Cys^†	nt	nt
FH20 site	Arg1182Ser^†	↓	↓
FH20 site	Trp1183Leu^†	↓	↓
FH20 site	Thr1184Arg^†	↓	↑
FH20 site	Arg1203Trp^†	↓	↓
FH20 site	Gly1204Glu^†	nt	nt
Heparin site?	Gly1194Asp^†	nt	nt
Heparin site	Arg1206Cys	↓	↓
Heparin site	Arg1210Cys	↓	↓
Heparin site	Arg1215Gln/Gly	↓	↓
Next to heparin site?	Leu1189Arg	↔	↑
Next to heparin site?	Glu1198Ala	↔	↑
aHUS mutations on C3d surface
C3d^FH19	Asp122Asn^†	↓
C3d^FH19	Gln168Lys^†	↓
C3d^FH20	Arg49Leu^†	nt
C3d^FH20	Ala101Val^†	↓
Next to C3d^FH19	Ile164Thr^†	nt

*Details of functional analyses and references are found in Tables S2 and S3. ↓, binding diminished because of the mutation; ↔, no effect; ↑, enhanced binding; nt, not tested.

^†Mutants discussed in this report. Buried mutations likely to disrupt the fold are not listed: Val1134Gly, Glu1135Asp, Trp1157Arg, Cys1163Trp, Val1168Glu, Ile1169Leu, Ile1170Val, Ser1191Leu/Trp, Val1197Ala, Phe1199Ser, and Pro1226Ser for FH19–20 and Cys165Trp for the C3d part of C3b.