1dsx: Difference between revisions
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'''KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT''' | '''KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT''' | ||
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[[Category: Lin, Y F.]] | [[Category: Lin, Y F.]] | ||
[[Category: Mobley, B C.]] | [[Category: Mobley, B C.]] | ||
[[Category: | [[Category: Assembly domain]] | ||
[[Category: | [[Category: Tetramer]] | ||
[[Category: | [[Category: Voltage-gated potassium channel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:14:08 2008'' | |||
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Revision as of 14:14, 2 May 2008
KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT
OverviewOverview
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.
About this StructureAbout this Structure
1DSX is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 14:14:08 2008