1qdv: Difference between revisions

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

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

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~~'''~~N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131~~'''~~

===N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131===

~~==Overview==~~

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~~Kv voltage-gated potassium channels share a cytoplasmic assembly domain~~, ~~T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However~~, ~~structural alterations of these mutants leave open~~ the ~~question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically~~ on ~~residues~~ at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. ~~Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel~~. ~~Together~~, ~~these data suggest that structural changes involving the buried polar T1 surfaces play a key role in~~ the ~~conformational changes leading to channel opening~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11007484}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11007484 is the PubMed ID number.

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==About this Structure==

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[[Category: Tetramerization domain]]

[[Category: Voltage-gated potassium channel]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 06~~:10:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:05:59 2008''

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-[[Image:1qdv.jpg|left|200px]]
+{{Seed}}
+[[Image:1qdv.png|left|200px]]
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@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qdv|  PDB=1qdv  |  SCENE=  }}
-'''N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131'''
+===N-TERMINAL DOMAIN, VOLTAGE-GATED POTASSIUM CHANNEL KV1.2 RESIDUES 33-131===
-==Overview==
+<!--
-Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening.
+The line below this paragraph, {{ABSTRACT_PUBMED_11007484}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11007484 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11007484}}
 ==About this Structure==
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 [[Category: Tetramerization domain]]
 [[Category: Voltage-gated potassium channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:10:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:05:59 2008''