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

TABLE II.

Biophysical Properties of hKv2.1/hKv1.5 Chimeric Constructs

S4-S5 linker S6
hKv1.5 K G L Q I L G K T L Q A S M R ll P V P V I V S N F N Y F Y H R E T D H E E
hKv2.1 T S F R R Y N ll I I N S E K E Q K R Q K
L45Kv2.1inKv1.5 T S F R R Y N ll
L45mutant1 S F R R Y N ll
L45mutant2 F R R Y N ll
L45mutant3 R R Y N ll
L45mutant4 F R R ll
L45mutant5 R R ll
K425F+R432N F N ll
L45S6Kv2.1inKv1.5 T S F R R Y N ll I I N S E K E Q K R Q K
S6Kv2.1inKv1.5 ll I I N S E K E Q K R Q K
Kv1.5chimera1 T S F R R Y N ll I I N S E
Kv1.5chimera2 T S F R R Y N ll N S E K E Q K R Q K
Kv1.5chimera3 T S F R R Y N ll I I K E Q K R Q K
Kv1.5chimera4 T S F R R Y N ll I K E Q K R Q K
Kv1.5chimera5 T S F R R Y N ll I Q K R Q K
Kv1.5chimera6 T S F R R Y N ll I Q K R
Kv1.5chimera7 T S F R R Y N ll I K R
Kv1.5chimera8 T S F R R Y N ll I Q K
Kv1.5chimera9 F N ll I I N S E K E Q K R Q K
Kv1.5chimera10 F N ll I Q K R
I
V1/2 (mV)
k (mV)
τa (ms)
τd (ms)
n
V1/2,i (mV)
ki (mV)
n
hKv1.5 ++ −14.3 ± 1.0 5.8 ± 0.2 3.5 ± 0.2 24.9 ± 2.5 9 −23.2 ± 1.3 3.9 ± 0.1 8
hKv2.1 ++ 12.3 ± 1.4 9.5 ± 0.6 33.8 ± 2.9 29.2 ± 2.2/170 ± 18 9 −15.9 ± 1.2 7.2 ± 0.6 5
L45Kv2.1inKv1.5
L45mutant1
L45mutant2
L45mutant3 + −20.6 ± 1.6 7.1 ± 0.2 10.1 ± 1.2 20.9 ± 3.2 7 −30.6 ± 1.1 4.1 ± 0.1 6
L45mutant4 + 11.1 ± 3.8 9.6 ± 1.0 3.9 ± 0.4 4.5 ± 0.9 6 −5.8 ± 1.6 5.0 ± 0.7 6
L45mutant5 + −8.7 ± 2.4 9.8 ± 0.8 3.9 ± 0.2 2.0 ± 0.3 9 −16.9 ± 1.8 6.4 ± 0.4 8
K425F+R432N +/− 0.8 ± 2.9 7.0 ± 0.8 4.7 ± 0.4 ND 3 ND ND
L45S6Kv2.1inKv1.5 + −8.4 ± 1.4 6.2 ± 0.2 48.1 ± 3.3 170 ± 17 5 −18.4 ± 1.2 4.1 ± 0.4 3
S6Kv2.1inKv1.5 ++ 1.1 ± 2.5 6.0 ± 0.5 14.9 ± 2.0 395 ± 35 8 −8.7 ± 2.4 4.9 ± 0.3 5
Kv1.5chimera1
Kv1.5chimera2
Kv1.5chimera3 + −13.9 ± 1.1 7.4 ± 0.4 39.9 ± 4.2 234 ± 40 7 −27.5 ± 0.6 5.4 ± 0.1 4
Kv1.5chimera4 + −23.7 ± 2.3 6.0 ± 0.4 13.0 ± 1.4 513 ± 41 5 −37.1 ± 3.0 4.2 ± 0.6 4
Kv1.5chimera5 + −31.3 ± 1.5 5.7 ± 0.6 10.6 ± 1.0 356 ± 52 6 −44.9 ± 1.3 4.8 ± 0.4 5
Kv1.5chimera6 + −16.4 ± 1.4 7.3 ± 0.3 10.0 ± 0.9 306 ± 13 6 −31.2 ± 2.0 4.5 ± 0.4 5
Kv1.5chimera7
Kv1.5chimera8
Kv1.5chimera9 ++ 0.1 ± 1.3 6.0 ± 0.4 8.3 ± 0.9 366 ± 48 6 −11.8 ± 1.2 5.4 ± 0.4 5
Kv1.5chimera10 ++ −12.4 ± 0.6 6.5 ± 0.3 4.6 ± 0.4 211 ± 18 9 −27.0 ± 0.6 4.0 ± 0.2 9

The L45 and S6T sequence of hKv1.5 is shown on top, above the hKv2.1 sequence. Mutant constructs were created in an hKv1.5 background with the respective substitutions set in bold. A + or − in column I indicates the presence or absence of time-dependent ionic current in the voltage range of −130 to +130 mV. The amount of plus signs represents the amplitude of K+ current recorded. For the double mutant K425F+R432N, +/− indicates that only very small time-dependent currents were observed with a maximal current amplitude of ∼50 pA with 7 μg cDNA transfected. V1/2, k, and time constants τa at V1/2 +60 mV and τd at V1/2 −40 mV were obtained as in Table I. ND, not determined.