1zwi: Difference between revisions

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[[Image:1zwi.~~gif~~|left|200px]]

[[Image:1zwi.png|left|200px]]

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~~'''~~Structure of mutant KcsA potassium channel~~'''~~

===Structure of mutant KcsA potassium channel===

~~==Overview==~~

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~~We show that in the potassium channel KcsA~~, ~~proton-dependent activation is followed by an inactivation process similar to C-type inactivation~~, ~~and this process is suppressed by an E71A mutation in~~ the ~~pore helix. EPR spectroscopy demonstrates that~~ the ~~inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements~~ at ~~the selectivity filter~~. ~~Two E71A crystal structures obtained at 2~~.~~5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of~~ the ~~range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16532009}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16532009 is the PubMed ID number.

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==About this Structure==

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[[Category: Transmembrane protein]]

[[Category: X-ray crystallography]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3~~ 18:09:53 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:01:00 2008''

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-[[Image:1zwi.gif|left|200px]]
+{{Seed}}
+[[Image:1zwi.png|left|200px]]
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 {{STRUCTURE_1zwi|  PDB=1zwi  |  SCENE=  }}
-'''Structure of mutant KcsA potassium channel'''
+===Structure of mutant KcsA potassium channel===
-==Overview==
+<!--
-We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.
+The line below this paragraph, {{ABSTRACT_PUBMED_16532009}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16532009 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16532009}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Transmembrane protein]]
 [[Category: X-ray crystallography]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:09:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:01:00 2008''