1s6c

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[[Image:1s6c.jpg|left|200px]]
[[Image:1s6c.jpg|left|200px]]
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{{Structure
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|PDB= 1s6c |SIZE=350|CAPTION= <scene name='initialview01'>1s6c</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1s6c", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>
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|ACTIVITY=
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|GENE= KChIP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), KCND2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|DOMAIN=
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{{STRUCTURE_1s6c| PDB=1s6c | SCENE= }}
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|RELATEDENTRY=[[1nn7|1NN7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6c OCA], [http://www.ebi.ac.uk/pdbsum/1s6c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s6c RCSB]</span>
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'''Crystal structure of the complex between KChIP1 and Kv4.2 N1-30'''
'''Crystal structure of the complex between KChIP1 and Kv4.2 N1-30'''
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[[Category: Qian, Y.]]
[[Category: Qian, Y.]]
[[Category: Zhou, W.]]
[[Category: Zhou, W.]]
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[[Category: ef-hand]]
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[[Category: Ef-hand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:21:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:38:01 2008''
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Revision as of 05:21, 3 May 2008

Image:1s6c.jpg

Template:STRUCTURE 1s6c

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. 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 Page seeded by OCA on Sat May 3 08:21:27 2008

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