3bj4

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(New page: 200px<br /><applet load="3bj4" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bj4, resolution 2.00&Aring;" /> '''The KCNQ1 (Kv7.1) C-...)
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==Overview==
==Overview==
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The Kv7 subfamily of voltage-dependent potassium channels, distinct from, other subfamilies by dint of its large intracellular C-terminus, acts to, regulate excitability in cardiac and neuronal tissues. KCNQ1 (Kv7.1), the, founding subfamily member, encodes a channel subunit directly implicated, in genetic disorders such as the long QT (LQT) syndrome, a cardiac, pathology responsible for arrhythmias. We have used a recombinant protein, preparation of the C-terminus to probe the structure and function of this, domain and its individual modules. The C-terminus proximal half associates, with one calmodulin (CaM) constitutively bound to each subunit where CaM, is critical for proper folding of the whole intracellular domain. The, distal half directs tetramerization, employing tandem coiled-coils. The, first coiled-coil complex is dimeric that undergoes, concentration-dependent self-association to form a dimer of dimers. The, outer coiled-coil is parallel tetrameric, whose details have been, elucidated based on 2.0 A crystallographic data. Both coiled-coils act in, a coordinate fashion to mediate the formation and stabilization of the, tetrameric distal half. Functional studies including characterization of, structure-based and LQT mutants prove the requirement for both modules and, point to complex roles for these modules including folding, assembly, trafficking and regulation.
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The Kv7 subfamily of voltage-dependent potassium channels, distinct from other subfamilies by dint of its large intracellular C-terminus, acts to regulate excitability in cardiac and neuronal tissues. KCNQ1 (Kv7.1), the founding subfamily member, encodes a channel subunit directly implicated in genetic disorders such as the long QT (LQT) syndrome, a cardiac pathology responsible for arrhythmias. We have used a recombinant protein preparation of the C-terminus to probe the structure and function of this domain and its individual modules. The C-terminus proximal half associates with one calmodulin (CaM) constitutively bound to each subunit where CaM is critical for proper folding of the whole intracellular domain. The distal half directs tetramerization, employing tandem coiled-coils. The first coiled-coil complex is dimeric that undergoes concentration-dependent self-association to form a dimer of dimers. The outer coiled-coil is parallel tetrameric, whose details have been elucidated based on 2.0 A crystallographic data. Both coiled-coils act in a coordinate fashion to mediate the formation and stabilization of the tetrameric distal half. Functional studies including characterization of structure-based and LQT mutants prove the requirement for both modules and point to complex roles for these modules including folding, assembly, trafficking and regulation.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hirsch, J.A.]]
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[[Category: Hirsch, J A.]]
[[Category: Wiener, R.]]
[[Category: Wiener, R.]]
[[Category: NI]]
[[Category: NI]]
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[[Category: voltage-gated channel]]
[[Category: voltage-gated channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:11:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:06:05 2008''

Revision as of 17:06, 21 February 2008

Image:3bj4.jpg

3bj4, resolution 2.00Å

Drag the structure with the mouse to rotate

The KCNQ1 (Kv7.1) C-terminus, a multi-tiered scaffold for subunit assembly and protein interaction

Overview

The Kv7 subfamily of voltage-dependent potassium channels, distinct from other subfamilies by dint of its large intracellular C-terminus, acts to regulate excitability in cardiac and neuronal tissues. KCNQ1 (Kv7.1), the founding subfamily member, encodes a channel subunit directly implicated in genetic disorders such as the long QT (LQT) syndrome, a cardiac pathology responsible for arrhythmias. We have used a recombinant protein preparation of the C-terminus to probe the structure and function of this domain and its individual modules. The C-terminus proximal half associates with one calmodulin (CaM) constitutively bound to each subunit where CaM is critical for proper folding of the whole intracellular domain. The distal half directs tetramerization, employing tandem coiled-coils. The first coiled-coil complex is dimeric that undergoes concentration-dependent self-association to form a dimer of dimers. The outer coiled-coil is parallel tetrameric, whose details have been elucidated based on 2.0 A crystallographic data. Both coiled-coils act in a coordinate fashion to mediate the formation and stabilization of the tetrameric distal half. Functional studies including characterization of structure-based and LQT mutants prove the requirement for both modules and point to complex roles for these modules including folding, assembly, trafficking and regulation.

About this Structure

3BJ4 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The KCNQ1 (Kv7.1) C-terminus, a multi-tieredscaffold for subunit assembly and protein interaction., Wiener R, Haitin Y, Shamgar L, Fernandez-Alonso MC, Martos A, Chomsky-Hecht O, Rivas G, Attali B, Hirsch JA, J Biol Chem. 2007 Dec 29;. PMID:18165683

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