Source:http://linkedlifedata.com/resource/pubmed/id/15109256
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
|
pubmed:dateCreated |
2004-4-27
|
pubmed:abstractText |
The hydrophobic cell membrane interior presents a large energy barrier for ions to permeate. Potassium channels reduce this barrier by creating a water-filled cavity at the middle of their ion conduction pore to allow ion hydration and by directing the C-terminal "end charge" of four alpha-helices toward the water-filled cavity. Here we have studied the interaction of monovalent cations with the cavity of the KcsA K(+) channel using X-ray crystallography. In these studies, Tl(+) was used as an analogue for K(+) and the total ion-stabilization energy for Tl(+) in the cavity was estimated by measuring its binding affinity. Binding affinity for the Na(+) ion was also measured, revealing a weak selectivity ( approximately 7-fold) favoring Tl(+) over Na(+). The structures of the cavity containing Na(+), K(+), Tl(+), Rb(+), and Cs(+) are compared. These results are consistent with a fairly large (more negative than -100 mV) electrostatic potential inside the cavity, and they also imply the presence of a weak nonelectrostatic component to a cation's interaction with the cavity.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cesium,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/Rubidium,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Thallium
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
43
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4978-82
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:15109256-Cell Membrane,
pubmed-meshheading:15109256-Cesium,
pubmed-meshheading:15109256-Crystallography, X-Ray,
pubmed-meshheading:15109256-Fourier Analysis,
pubmed-meshheading:15109256-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:15109256-Ions,
pubmed-meshheading:15109256-Osmolar Concentration,
pubmed-meshheading:15109256-Potassium,
pubmed-meshheading:15109256-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:15109256-Protein Structure, Secondary,
pubmed-meshheading:15109256-Rubidium,
pubmed-meshheading:15109256-Sodium,
pubmed-meshheading:15109256-Static Electricity,
pubmed-meshheading:15109256-Thallium
|
pubmed:year |
2004
|
pubmed:articleTitle |
Ion binding affinity in the cavity of the KcsA potassium channel.
|
pubmed:affiliation |
Howard Hughes Medical Institute and Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|