Abstract:
:We report results from automated docking and microscopic molecular dynamics simulations of the tetraethylammonium (TEA) complexes with KcsA. Binding modes and energies for TEA binding at the external and internal sides of the channel pore are examined utilising the linear interaction energy method. Effects of the channel ion occupancy (based on our previous results for the ion permeation mechanisms) on the binding energies are considered. Calculations show that TEA forms stable complexes at both the external and internal entrances of the selectivity filter. Furthermore, the effects of the Y82V mutation are evaluated and the results show, in agreement with experimental data, that the mutant has a significantly reduced binding affinity for TEA at the external binding site, which is attributed to stabilising hydrophobic interactions between the ligand and the tyrosines.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Luzhkov VB,Aqvist Jdoi
10.1016/s0014-5793(01)02381-xkeywords:
subject
Has Abstractpub_date
2001-04-27 00:00:00pages
191-6issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02381-Xjournal_volume
495pub_type
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