Our understanding of ion permeation through K+ channels, and by extension through other channels, is advancing rapidly. New structural studies, together with computer simulations, have provided profound insights into ion conduction mechanisms. When the crystal structure of the bacterial channel protein KcsA was first solved in 1998 [1], it provided us with our first view of an ion channel at atomic res-olution. The structure, determined at the relatively modest resolution of 3.2 Å, revealed the basic archi-tecture of the channel: an extracellular selectivity filter, a central cavity and an intracellular gate (Figure 1). The importance of KcsA lies in the conservation of this basic pore structure between KcsA and other classes of K+ channels...
AbstractPotassium channels have been studied intensively in terms of the relationship between molecu...
The ability of biological ion channels to conduct selected ions across cell membranes is critical fo...
The potassium channel from Streptomyces lividans is an integral membrane protein with sequence simil...
Our understanding of ion permeation through K(+) channels, and by extension through other channels, ...
AbstractCrystal structures have been solved for the transbilayer pore domain of a bacterial K+ chann...
AbstractOur understanding of ion permeation through K+ channels, and by extension through other chan...
Potassium channels enable K(+) ions to move passively across biological membranes. Multiple nanoseco...
Potassium channels have been studied intensively in terms of the relationship between molecular stru...
AbstractPotassium channels enable K+ ions to move passively across biological membranes. Multiple na...
ABSTRACT Potassium channels enable K1 ions to move passively across biological membranes. Multiple n...
AbstractPotassium channels selectively catalyze potassium transport across cell membranes. Over the ...
AbstractInteractions of Na+, K+, Rb+, and Cs+ ions within the selectivity filter of a potassium chan...
The bacterial K+ channel KcsA can be used to help elucidate questions about channel inactivation and...
Determination of the crystal structure of the KcsA potassium channel and its subsequent refinement a...
Ion channels control the movement of ions allowing specific ions to pass across biological membranes...
AbstractPotassium channels have been studied intensively in terms of the relationship between molecu...
The ability of biological ion channels to conduct selected ions across cell membranes is critical fo...
The potassium channel from Streptomyces lividans is an integral membrane protein with sequence simil...
Our understanding of ion permeation through K(+) channels, and by extension through other channels, ...
AbstractCrystal structures have been solved for the transbilayer pore domain of a bacterial K+ chann...
AbstractOur understanding of ion permeation through K+ channels, and by extension through other chan...
Potassium channels enable K(+) ions to move passively across biological membranes. Multiple nanoseco...
Potassium channels have been studied intensively in terms of the relationship between molecular stru...
AbstractPotassium channels enable K+ ions to move passively across biological membranes. Multiple na...
ABSTRACT Potassium channels enable K1 ions to move passively across biological membranes. Multiple n...
AbstractPotassium channels selectively catalyze potassium transport across cell membranes. Over the ...
AbstractInteractions of Na+, K+, Rb+, and Cs+ ions within the selectivity filter of a potassium chan...
The bacterial K+ channel KcsA can be used to help elucidate questions about channel inactivation and...
Determination of the crystal structure of the KcsA potassium channel and its subsequent refinement a...
Ion channels control the movement of ions allowing specific ions to pass across biological membranes...
AbstractPotassium channels have been studied intensively in terms of the relationship between molecu...
The ability of biological ion channels to conduct selected ions across cell membranes is critical fo...
The potassium channel from Streptomyces lividans is an integral membrane protein with sequence simil...