1eof: Difference between revisions
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==CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN== | ==CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN== | ||
<StructureSection load='1eof' size='340' side='right' caption='[[1eof]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='1eof' size='340' side='right'caption='[[1eof]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1eof]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplca Aplca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EOF FirstGlance]. <br> | <table><tr><td colspan='2'>[[1eof]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplca Aplca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EOF FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1eof" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1eof" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Potassium Channel|Potassium Channel]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aplca]] | [[Category: Aplca]] | ||
[[Category: Large Structures]] | |||
[[Category: Choe, S]] | [[Category: Choe, S]] | ||
[[Category: Cushman, S J]] | [[Category: Cushman, S J]] | ||
Revision as of 12:22, 6 November 2019
CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAINCRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe T1 domain, a highly conserved cytoplasmic portion at the N-terminus of the voltage-dependent K+ channel (Kv) alpha-subunit, is responsible for driving and regulating the tetramerization of the alpha-subunits. Here we report the identification of a set of mutations in the T1 domain that alter the gating properties of the Kv channel. Two mutants produce a leftward shift in the activation curve and slow the channel closing rate while a third mutation produces a rightward shift in the activation curve and speeds the channel closing rate. We have determined the crystal structures of T1 domains containing these mutations. Both of the leftward shifting mutants produce similar conformational changes in the putative membrane facing surface of the T1 domain. These results suggest that the structure of the T1 domain in this region is tightly coupled to the channel's gating states. Voltage dependent activation of potassium channels is coupled to T1 domain structure.,Cushman SJ, Nanao MH, Jahng AW, DeRubeis D, Choe S, Pfaffinger PJ Nat Struct Biol. 2000 May;7(5):403-7. PMID:10802739[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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