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1s6c
From Proteopedia
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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 CA 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
Page seeded by OCA on Wed Nov 21 02:09:02 2007
Categories: Protein complex | Rattus norvegicus | Choe, S. | Kunjilwar, K. | Pfaffinger, P.J. | Qian, Y. | Zhou, W. | CA | Ef-hand
