Article abstract
Nature Neuroscience 10, 32 - 39 (2007)
Published online: 24 December 2006 | doi:10.1038/nn1822
There is a Corrigendum (February 2007) associated with this Article.
Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits
Huayi Wang1,4, Yan Yan2,4, Qun Liu3, Yanhua Huang2, Yue Shen1, Linjie Chen1, Yi Chen2, Qiuyue Yang3, Quan Hao3, KeWei Wang2 & Jijie Chai1
Abstract
KChIPs coassemble with pore-forming Kv4 
subunits to form a native complex in the brain and heart and regulate the expression and gating properties of Kv4 K+ channels, but the mechanisms underlying these processes are unknown. Here we report a co-crystal structure of the complex of human Kv4.3 N-terminus and KChIP1 at a 3.2-Å resolution. The structure reveals a unique clamping action of the complex, in which a single KChIP1 molecule, as a monomer, laterally clamps two neighboring Kv4.3 N-termini in a 4:4 manner, forming an octamer. The proximal N-terminal peptide of Kv4.3 is sequestered by its binding to an elongated groove on the surface of KChIP1, which is indispensable for the modulation of Kv4.3 by KChIP1, and the same KChIP1 molecule binds to an adjacent T1 domain to stabilize the tetrameric Kv4.3 channels. Taken together with biochemical and functional data, our findings provide a structural basis for the modulation of Kv4 by KChIPs.
- National Institute of Biological Sciences, No. 7 Science Park Road, Beijing 102206, China.
- Neuroscience Research Institute, Department of Neurobiology, Key Laboratory for Neuroscience of the Ministry of Education, Center for Protein Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing 100083, China.
- Cornell High-Energy Synchrotron Source, Cornell University, Ithaca, New York 14853, USA.
- These authors contributed equally to this work.
Correspondence to: KeWei Wang2 e-mail: wangkw@bjmu.edu.cn
Correspondence to: Jijie Chai1 e-mail: chaijijie@nibs.ac.cn
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