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. 2008 Dec;132(6):667–680. doi: 10.1085/jgp.200810048

TABLE III.

Biophysical Properties of Individual Substitutions in hKv1.5

hKv1.5 K G L Q I L G K T L Q A S M R E
I I I I I I I I
position 418 420 422 424 426 428 430 432
(380) (382) (384) (386) (388) (390) (392) (392)
Activation Deactivation Inactivation
V1/2 (mV)
k (mV)
τa (ms)
τd (ms)
V1/2,i (mV)
ki (mV)
n
K418T 1.5 ± 1.5 7.3 ± 0.6 4.5 ± 0.4 22.8 ± 3.0 −8.2 ± 0.7 4.9 ± 0.3 6
I422S −26.4 ± 1.9 6.9 ± 0.6 12.6 ± 0.9 475 ± 27 −38.9 ± 1.0 4.5 ± 0.2 5
I422A −24.1 ± 2.3 7.0 ± 0.7 5.7 ± 0.4 277 ± 52 −33.7 ± 1.7 5.8 ± 0.3 7
I422W no current
I422R no current
K425E −10.1 ± 1.9 6.0 ± 0.3 4.3 ± 0.3 18.9 ± 3.2 −16.4 ± 1.4 3.6 ± 0.3 5
K425F −5.2 ± 2.7 6.2 ± 1.3 7.8 ± 1.0 ND ND ND 3
K425A 12.2 ± 1.6 7.0 ± 0.3 5.7 ± 0.8 19.2 ± 1.9 2.9 ± 1.5 5.5 ± 0.3 6
T426A −1.5 ± 2.0 6.6 ± 0.3 3.6 ± 0.2 6.6 ± 0.8 −13.9 ± 2.6 4.5 ± 0.4 5
T426W no current
T426R no current
Q428R −9.7 ± 1.4 6.5 ± 0.2 5.0 ± 0.8 22.0 ± 5.2 −19.3 ± 0.6 5.0 ± 0.1 5
A429R −8.2 ± 1.8 7.1 ± 0.5 7.0 ± 0.6 4.4 ± 0.5 −16.2 ± 2.6 5.2 ± 0.3 5
M431F −11.1 ± 1.4 5.9 ± 0.3 5.5 ± 0.9 16.1 ± 1.4 −16.3 ± 0.9 4.9 ± 0.3 6
R432E −9.4 ± 0.6 4.9 ± 0.3 3.0 ± 0.3 13.7 ± 0.3 −14.0 ± 1.5 4.1 ± 0.2 4
R432N −1.6 ± 1.2 5.8 ± 0.2 4.4 ± 0.5 57.0 ± 5.3 −7.5 ± 1.4 4.5 ± 0.2 8
R432F 17.4 ± 1.3 7.0 ± 0.5 5.9 ± 0.7 12.5 ± 0.5 2.0 ± 1.1 4.3 ± 0.3 7
V514I −5.1 ± 1.7 5.4 ± 0.7 4.5 ± 0.5 223 ± 19 −12.4 ± 1.4 3.6 ± 0.3 5
Y521E −14.9 ± 1.4 5.3 ± 0.4 3.5 ± 0.3 11.9 ± 1.1 −22.8 ± 2.1 3.7 ± 0.4 5
H524K −5.0 ± 1.6 4.6 ± 0.4 4.0 ± 0.4 26.6 ± 2.7 −11.5 ± 1.3 4.0 ± 0.1 5
R525E −16.5 ± 0.9 5.6 ± 0.4 3.5 ± 0.2 25.8 ± 2.1 −26.4 ± 0.9 3.2 ± 0.1 6
E526Q −9.6 ± 0.3 5.1 ± 0.3 4.8 ± 0.6 13.8 ± 1.8 −16.8 ± 1.2 4.5 ± 0.2 4
T527K −7.1 ± 0.3 5.1 ± 0.2 4.2 ± 0.5 17.9 ± 3.2 −12.3 ± 1.4 3.8 ± 0.3 5
D528R −10.9 ± 1.5 5.3 ± 0.5 4.7 ± 0.4 26.6 ± 2.6 −18.4 ± 0.6 4.0 ± 0.2 7
H529Q −3.7 ± 1.2 5.0 ± 0.4 4.2 ± 0.5 18.8 ± 2.3 −9.0 ± 2.0 4.1 ± 0.4 6
E531K −9.9 ± 2.8 5.6 ± 0.6 4.9 ± 0.5 20.4 ± 1.6 −17.0 ± 1.1 3.5 ± 0.2 5

Sequence of L45 from hKv1.5 on top with Shaker numbering between parentheses. All mutations were done in an hKv1.5 background, and V1/2, k, and t were obtained as in Table I. ND, not determined.