1dsx

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[[Image:1dsx.gif|left|200px]]
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{{Seed}}
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[[Image:1dsx.png|left|200px]]
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{{STRUCTURE_1dsx| PDB=1dsx | SCENE= }}
{{STRUCTURE_1dsx| PDB=1dsx | SCENE= }}
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'''KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT'''
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===KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT===
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==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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11007484}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11007484 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11007484}}
==About this Structure==
==About this Structure==
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[[Category: Tetramer]]
[[Category: Tetramer]]
[[Category: Voltage-gated potassium channel]]
[[Category: Voltage-gated potassium channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:14:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:34:15 2008''

Revision as of 20:34, 30 June 2008

Image:1dsx.png

Template:STRUCTURE 1dsx

KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT

Template:ABSTRACT PUBMED 11007484

About this Structure

1DSX is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel., Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM, Cell. 2000 Sep 1;102(5):657-70. PMID:11007484

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