. Author manuscript; available in PMC: 2009 Sep 12.

Published in final edited form as: J Mol Biol. 2008 Jun 20;381(4):956–974. doi: 10.1016/j.jmb.2008.06.041

TABLE 2.

Binding affinity of CCR5 inhibitors to mutant CCR5s

		K_D value (nM)
Mutant CCR5 on CHO cells		AK530	AK317	APL
Wild type		1.4 ± 0.9	16.7 ± 7.5	3.6 ± 1.4
D11A	NH₂-terminus	1.1 ± 0.5	14.6 ± 1.9	3.0 ± 0.6^a
Y37A	TM1	>100	>100^b	12.8 ± 0.9
P84H	TM2	37.3 ± 6.3	>100	>100
C101A	TM3	>100	>100	>100
L104D	TM3	6.8 ± 0.7	93.3 ± 26.4	18.3 ± 3.6
Y108A	TM3	60.7 ± 26.2	>100	19.8 ± 4.4^a
F109A	TM3	>100	>100	>100
F112L	TM3	5.4 ± 2.1	14.7 ± 2.5	4.0 ± 2.6 ^a
F112Y	TM3	5.2 ± 3.4	21.1 ± 8.9	6.8 ± 1.1 ^a
F113A	TM3	2.4 ± 0.3	43.3 ± 7.4	13.3 ± 2.3 ^a
F113Y	TM3	2.8 ± 0.5	48.2 ± 10.2	12.9 ± 3.1
G163A	TM4	5.9 ± 2.6	14.7 ± 0.1	8.0 ± 4.2 ^a
G163R	TM4	>100	>100	>200 ^a
R168A	ECL2	2.2 ± 0.7	24.6 ± 4.1	14.1 ± 9.4
K171A/E172A	ECL2	3.5 ± 1.2	14.7 ± 0.1	2.8 ± 0.1 ^a
C178A	ECL2	>100	>100	>200 ^a
S180A	ECL2	7.4 ± 1.4	34.5 ± 7.9	5.7 ± 1.2 ^a
S180T	ECL2	1.4 ± 0.6	14.9 ± 1.7	1.5 ± 0.6 ^a
S180E	ECL2	5.7 ± 2.3	61.8 ± 22.9	13.9 ± 1.7 ^a
Y184A/S185A	ECL2	2.2 ± 2.3	14.8 ± 0.2	2.0 ± 0.8 ^a
Y184A/S185A/Q186A/Y187A	ECL2	2.2 ± 0.4	22.0 ± 4.2	2.0 ± 0.6 ^a
Q186A/Y187A	ECL2	2.3 ± 0.1	14.4 ± 2.2	2.8 ± 0.5 ^a
Q188A	ECL2	1.9 ± 1.3	14.6 ± 3.6	6.6 ± 1.4 ^a
K191A	ECL2-TM5	6.0 ± 3.8	>100	>200 ^a
K191R	ECL2-TM5	5.2 ± 2.8	22.2 ± 7.7	9.0 ± 5.6 ^a
K191N	ECL2-TM5	12.5 ± 3.3	>100	14.2 ± 1.1 ^a
T195A	TM5	5.6 ± 3.9	14.7 ± 0.1	48.1 ± 4.3
T195P	TM5	>100	>100	>100
T195S	TM5	>100	>100	>100
K197A	TM5	7.6 ± 3.7	58.3 ± 18.7	10.7 ± 3.5
I198A	TM5	9.8 ± 2.2	>100	24.6 ± 4.8 ^a
W248A	TM6	43.4 ± 4.5	>100	29.8 ± 4.6
Y251A	TM6	>100	>100	36.5 ± 9.5 ^a
E283A	TM7	19.1 ± 2.5	>100	>200 ^a
M287A	TM7	2.4 ± 1.4	16.1 ± 2.1	6.8 ± 2.3 ^a
M287E	TM7	62.7 ± 17.8	87.1 ± 0.6	14.8 ± 1.7 ^a

Data from Maeda et al. ²²

K_D values more than 5-fold compared to that with CCR5_WT are shown in bold.