1s6c

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(New page: 200px<br /><applet load="1s6c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s6c, resolution 2.0&Aring;" /> '''Crystal structure of ...)
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[[Image:1s6c.jpg|left|200px]]<br /><applet load="1s6c" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s6c.jpg|left|200px]]<br /><applet load="1s6c" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s6c, resolution 2.0&Aring;" />
caption="1s6c, resolution 2.0&Aring;" />
'''Crystal structure of the complex between KChIP1 and Kv4.2 N1-30'''<br />
'''Crystal structure of the complex between KChIP1 and Kv4.2 N1-30'''<br />
==Overview==
==Overview==
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Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact, directly with the N-terminal domain of three Shal-type voltage-gated, potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface, expression and function of Kv4 channels. Here we report a 2.0 Angstrom, crystal structure of the core domain of KChIP1 (KChIP1*) in complex with, the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a, clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each, shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix, (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed, nearly coaxially by these shells. As a result, the H10 of KChIP1 and, alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its, target peptides. Site-specific mutagenesis combined with functional, characterization shows that those interactions mediated by alpha1 and H10, are essential to the modulation of Kv4.2 by KChIPs.
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Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact directly with the N-terminal domain of three Shal-type voltage-gated potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface expression and function of Kv4 channels. Here we report a 2.0 Angstrom crystal structure of the core domain of KChIP1 (KChIP1*) in complex with the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. Site-specific mutagenesis combined with functional characterization shows that those interactions mediated by alpha1 and H10 are essential to the modulation of Kv4.2 by KChIPs.
==About this Structure==
==About this Structure==
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1S6C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S6C OCA].
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1S6C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6C OCA].
==Reference==
==Reference==
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[[Category: Choe, S.]]
[[Category: Choe, S.]]
[[Category: Kunjilwar, K.]]
[[Category: Kunjilwar, K.]]
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[[Category: Pfaffinger, P.J.]]
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[[Category: Pfaffinger, P J.]]
[[Category: Qian, Y.]]
[[Category: Qian, Y.]]
[[Category: Zhou, W.]]
[[Category: Zhou, W.]]
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[[Category: ef-hand]]
[[Category: ef-hand]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:09:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:30 2008''

Revision as of 12:58, 21 February 2008

Image:1s6c.jpg

1s6c, resolution 2.0Å

Drag the structure with the mouse to rotate

Crystal structure of the complex between KChIP1 and Kv4.2 N1-30

Overview

Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact directly with the N-terminal domain of three Shal-type voltage-gated potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface expression and function of Kv4 channels. Here we report a 2.0 Angstrom crystal structure of the core domain of KChIP1 (KChIP1*) in complex with the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. Site-specific mutagenesis combined with functional characterization shows that those interactions mediated by alpha1 and H10 are essential to the modulation of Kv4.2 by KChIPs.

About this Structure

1S6C is a Protein complex structure of sequences from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels., Zhou W, Qian Y, Kunjilwar K, Pfaffinger PJ, Choe S, Neuron. 2004 Feb 19;41(4):573-86. PMID:14980206

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