1S6C

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

Summary for 1S6C

• Entry DOI: 10.2210/pdb1s6c/pdb
• Related: 1NN7
• Descriptor: Kv4 potassium channel-interacting protein KChIP1b, Potassium voltage-gated channel subfamily D member 2, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: ef-hand, transport protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane; Peripheral membrane protein (By similarity): Q8R426; Cell membrane; Multi-pass membrane protein: Q63881
• Total number of polymer chains: 2
• Total formula weight: 24807.98

Authors

Zhou, W.,Qian, Y.,Kunjilwar, K.,Pfaffinger, P.J.,Choe, S. (deposition date: 2004-01-23, release date: 2004-02-24, Last modification date: 2024-11-20)

Primary citation

Zhou, W.,Qian, Y.,Kunjilwar, K.,Pfaffinger, P.J.,Choe, S.
Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels.
Neuron, 41:573-586, 2004

PubMed Abstract: 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.

PubMed: 14980206
DOI: 10.1016/S0896-6273(04)00045-5

Experimental method

X-RAY DIFFRACTION (2 Å)