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| {{STRUCTURE_1s6c| PDB=1s6c | SCENE= }} | | {{STRUCTURE_1s6c| PDB=1s6c | SCENE= }} |
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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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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14980206}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14980206 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14980206}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zhou, W.]] | | [[Category: Zhou, W.]] |
| [[Category: Ef-hand]] | | [[Category: Ef-hand]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:21:27 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:30:35 2008'' |
