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. 2004 Oct;87(4):2116–2130. doi: 10.1529/biophysj.104.040618

TABLE 1.

Postulated interactions of L45 residues with S5 or S6 residues (β-carbons <7 Å apart)

L45 residues S5 or S6 residues
Model of open conformation
H378 L403, F404, I464
 S379 L403, L399, I400
G481 A465*
L382 A465*, L468*, P473, V474
 Q383 L396
L385 L468*
 G386 L472*, I477
L389 L472*, F481
S389 L398*
 M393 F484, Y485
Resting conformation (model 1 of Fig. 4)
G381 I464*
L382 L399, I400, L403, T469, L472, P473
L385 I464*, V467*, L468*, P473
 G386 L496, P473
T388 L468*
L389 L468*, A472*, L472*, P473, I477
S392 L396*, L399*L472*,
Resting conformation (model 2, L45 more inward)
G381 L396, P473
L382 M393, L396, V476
L385 V476, I477, N480
 G386 N480
T388 L472*, P475*, I477, N480
L389 N480, F481, F484

Bold residues are conserved among Kv channels (red, orange, and yellow in Fig. 7 of accompanying article).

*

Interactions are within the same subunit. Residues were considered proximal if the distance between β-carbons was <7 Å.