Premium
THEMATICS analysis for functional ion channels
Author(s) -
Shehadi Ihsan A.
Publication year - 2007
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.21386
Subject(s) - kcsa potassium channel , mechanosensitive channels , ion channel , voltage gated ion channel , ion , chemistry , biophysics , light gated ion channel , potassium channel , stretch activated ion channel , membrane , chemical physics , nanotechnology , materials science , biochemistry , biology , receptor , organic chemistry
Abstract Ion channels, as a group of integral membrane proteins, span the cell membrane forming ion‐conducting pores that allow ions to traverse the hydrophobic lipid environment rapidly and selectively. The structure of the Streptomyces lividians (KcsA) and Mycobacterium tuberculosis ion channel (Mscl) potassium ion channel have provided the impetus and has helped further the understanding of the structural and functional studies of these channels. The KcsA adapts the voltage‐gated mechanism for opening and closing of the channel. While Mcsl represents the mechanosensitive model of the channels. However, the mechanism of the opening and closing of these channels are not fully understood. Electrostatic methods (THEMATICS) are used to locate the site where closing and opening of the channels are controlled. Two clusters of amino acid residues are identified in each of the previously mentioned active models where net charges play an important role in controlling the mechanism of the opening and closure of the ion channels. © 2007 Wiley Periodicals, Inc. Int J Quantum Chem, 2007