2i2r: Difference between revisions

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[[Image:2i2r.~~jpg~~|left|200px]]

[[Image:2i2r.png|left|200px]]

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~~'''~~Crystal structure of the KChIP1/Kv4.3 T1 complex~~'''~~

===Crystal structure of the KChIP1/Kv4.3 T1 complex===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_17057713}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17057713 is the PubMed ID number.

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==About this Structure==

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[[Category: Ncs protein]]

[[Category: Potassium channel]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 07~~:00:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:27:03 2008''

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-[[Image:2i2r.jpg|left|200px]]
+{{Seed}}
+[[Image:2i2r.png|left|200px]]
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 {{STRUCTURE_2i2r|  PDB=2i2r  |  SCENE=  }}
-'''Crystal structure of the KChIP1/Kv4.3 T1 complex'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17057713}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17057713 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17057713}}
 ==About this Structure==
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 [[Category: Ncs protein]]
 [[Category: Potassium channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:00:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:27:03 2008''