TY - JOUR
T1 - Single potassium ion seeks open channel for transmembrane travels
T2 - Tales from the KcsA structure
AU - Gouaux, Eric
N1 - Funding Information:
The work in the Gouaux lab is supported by grants from the National Institutes of Health (NIH), National Science Foundation (NSF) and Office of Naval Research (ONR). EG is an NSF Young Investigator and an Alfred P Sloan Research Fellow.
PY - 1998/10/15
Y1 - 1998/10/15
N2 - Potassium channels selectively catalyze potassium transport across cell membranes. Over the past five decades, a multitude of potassium channel models have been proposed. The recent crystal structure determination of the KcsA potassium channel confirms, corrects and expands our understanding of a fundamental biological catalyst, revealing the basis of exquisite selectivity and near diffusion-limited throughput.
AB - Potassium channels selectively catalyze potassium transport across cell membranes. Over the past five decades, a multitude of potassium channel models have been proposed. The recent crystal structure determination of the KcsA potassium channel confirms, corrects and expands our understanding of a fundamental biological catalyst, revealing the basis of exquisite selectivity and near diffusion-limited throughput.
UR - http://www.scopus.com/inward/record.url?scp=0032532160&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032532160&partnerID=8YFLogxK
U2 - 10.1016/S0969-2126(98)00122-1
DO - 10.1016/S0969-2126(98)00122-1
M3 - Article
C2 - 9782060
AN - SCOPUS:0032532160
SN - 0969-2126
VL - 6
SP - 1221
EP - 1226
JO - Structure
JF - Structure
IS - 10
ER -