1eof: Difference between revisions

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[[Image:1eof.~~jpg~~|left|200px]]

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

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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===

~~==Overview==~~

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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.

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==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~~:20:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:17:56 2008''

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-[[Image:1eof.jpg|left|200px]]
+{{Seed}}
+[[Image:1eof.png|left|200px]]
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@@ Line 9: / Line 10: @@
 {{STRUCTURE_1eof|  PDB=1eof  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN'''
+===CRYSTAL STRUCTURE OF THE N136A 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==
@@ Line 31: / Line 35: @@
 [[Category: Potassium channel]]
 [[Category: Proton transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:20:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:17:56 2008''