1eoe: Difference between revisions

Revision as of 01:18, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1eoe.png

Template:STRUCTURE 1eoe

CRYSTAL STRUCTURE OF THE V135R MUTANT OF A SHAKER T1 DOMAINCRYSTAL STRUCTURE OF THE V135R MUTANT OF A SHAKER T1 DOMAIN

Template:ABSTRACT PUBMED 10802739

About this StructureAbout this Structure

1EOE is a Single protein structure of sequence from Aplysia californica. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 01:17:55 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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+{{Seed}}
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-'''CRYSTAL STRUCTURE OF THE V135R MUTANT OF A SHAKER T1 DOMAIN'''
+===CRYSTAL STRUCTURE OF THE V135R MUTANT OF A SHAKER T1 DOMAIN===
-==Overview==
+<!--
-The 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10802739}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10802739 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10802739}}
 ==About this Structure==
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 [[Category: Potassium channel]]
 [[Category: Proton transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:20:43 2008''
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