2i2r
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 | + | Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 voltage-gated potassium channels and cytoplasmic calcium-sensor proteins (KChIPs). Here, we present X-ray crystallographic and small-angle X-ray scattering data that show that the KChIP1-Kv4.3 N-terminal cytoplasmic domain complex is a cross-shaped octamer bearing two principal interaction sites. Site 1 comprises interactions between a unique Kv4 channel N-terminal hydrophobic segment and a hydrophobic pocket formed by displacement of the KChIP H10 helix. Site 2 comprises interactions between a T1 assembly domain loop and the KChIP H2 helix. Functional and biochemical studies indicate that site 1 influences channel trafficking, whereas site 2 affects channel gating, and that calcium binding is intimately linked to KChIP folding and complex formation. Together, the data resolve how Kv4 channels and KChIPs interact and provide a framework for understanding how KChIPs modulate Kv4 function. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Findeisen, F.]] | [[Category: Findeisen, F.]] | ||
| - | [[Category: Jr., D | + | [[Category: Jr., D L.Minor.]] |
[[Category: Pioletti, M.]] | [[Category: Pioletti, M.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: potassium channel]] | [[Category: potassium channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:29 2008'' |
Revision as of 15:48, 21 February 2008
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Crystal structure of the KChIP1/Kv4.3 T1 complex
Overview
Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 voltage-gated potassium channels and cytoplasmic calcium-sensor proteins (KChIPs). Here, we present X-ray crystallographic and small-angle X-ray scattering data that show that the KChIP1-Kv4.3 N-terminal cytoplasmic domain complex is a cross-shaped octamer bearing two principal interaction sites. Site 1 comprises interactions between a unique Kv4 channel N-terminal hydrophobic segment and a hydrophobic pocket formed by displacement of the KChIP H10 helix. Site 2 comprises interactions between a T1 assembly domain loop and the KChIP H2 helix. Functional and biochemical studies indicate that site 1 influences channel trafficking, whereas site 2 affects channel gating, and that calcium binding is intimately linked to KChIP folding and complex formation. Together, the data resolve how Kv4 channels and KChIPs interact and provide a framework for understanding how KChIPs modulate Kv4 function.
About this Structure
2I2R is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with , and as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer., Pioletti M, Findeisen F, Hura GL, Minor DL Jr, Nat Struct Mol Biol. 2006 Nov;13(11):987-95. Epub 2006 Oct 22. PMID:17057713
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