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Article: Structural basis for modulation of Kv4 K + channels by auxiliary KChIP subunits

TitleStructural basis for modulation of Kv4 K + channels by auxiliary KChIP subunits
Authors
Issue Date2007
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/neuro/
Citation
Nature Neuroscience, 2007, v. 10 n. 1, p. 32-39 How to Cite?
AbstractKChIPs coassemble with pore-forming Kv4 α 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. © 2007 Nature Publishing Group.
Persistent Identifierhttp://hdl.handle.net/10722/91909
ISSN
2015 Impact Factor: 16.724
2015 SCImago Journal Rankings: 13.558
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Hen_HK
dc.contributor.authorYan, Yen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHuang, Yen_HK
dc.contributor.authorShen, Yen_HK
dc.contributor.authorChen, Len_HK
dc.contributor.authorChen, Yen_HK
dc.contributor.authorYang, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorWang, Ken_HK
dc.contributor.authorChai, Jen_HK
dc.date.accessioned2010-09-17T10:30:14Z-
dc.date.available2010-09-17T10:30:14Z-
dc.date.issued2007en_HK
dc.identifier.citationNature Neuroscience, 2007, v. 10 n. 1, p. 32-39en_HK
dc.identifier.issn1097-6256en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91909-
dc.description.abstractKChIPs coassemble with pore-forming Kv4 α 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. © 2007 Nature Publishing Group.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/neuro/en_HK
dc.relation.ispartofNature Neuroscienceen_HK
dc.titleStructural basis for modulation of Kv4 K + channels by auxiliary KChIP subunitsen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/nn1822en_HK
dc.identifier.pmid17187064-
dc.identifier.scopuseid_2-s2.0-33845875691en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845875691&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume10en_HK
dc.identifier.issue1en_HK
dc.identifier.spage32en_HK
dc.identifier.epage39en_HK
dc.identifier.isiWOS:000243096100013-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWang, H=12805598700en_HK
dc.identifier.scopusauthoridYan, Y=55239611900en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHuang, Y=23988825500en_HK
dc.identifier.scopusauthoridShen, Y=49762197700en_HK
dc.identifier.scopusauthoridChen, L=15753380200en_HK
dc.identifier.scopusauthoridChen, Y=7601447379en_HK
dc.identifier.scopusauthoridYang, Q=15754740400en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridWang, K=15836024700en_HK
dc.identifier.scopusauthoridChai, J=7202678942en_HK
dc.identifier.citeulike1014423-

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