dc.contributor.authorLi, Qingxin
dc.contributor.authorNg, Hui Qi
dc.contributor.authorYoon, Ho Sup
dc.contributor.authorKang, CongBao
dc.date.accessioned2016-07-12T05:01:24Z
dc.date.available2016-07-12T05:01:24Z
dc.date.issued2014
dc.identifier.citationLi, Q., Ng, H. Q., Yoon, H. S., & Kang, C. (2014). Insight into the molecular interaction between the cyclic nucleotide-binding homology domain and the eag domain of the hERG channel. FEBS Letters, 588(17), 2782-2788.en_US
dc.identifier.issn0014-5793en_US
dc.identifier.urihttp://hdl.handle.net/10220/40916
dc.description.abstractThe gating of the hERG channel is regulated by its eag domain through molecular interaction with either the cyclic nucleotide-binding homology domain (CNBHD) or the linker between transmembrane segments 4 and 5. Our NMR study on the purified CNBHD demonstrated that it contains nine β-strands and does not bind cAMP. We show that the eag domain binds to the CBND through an interface containing several disease-associated mutations. The N-terminal cap domain and R56 in the eag domain are important for the interaction with the CNBHD. Residues from the CNBHD that were affected by the interaction with the eag domain were also identified. A R56Q mutation does not cause major structural changes in the eag domain and showed reduced interaction with the CNBHD.en_US
dc.description.sponsorshipASTAR (Agency for Sci., Tech. and Research, S’pore)en_US
dc.language.isoenen_US
dc.relation.ispartofseriesFEBS Lettersen_US
dc.rights© 2014 Federation of European Biochemical Societies (Published by Elsevier B.V.).en_US
dc.subjecthERGen_US
dc.subjectCyclic nucleotide-binding homology domainen_US
dc.titleInsight into the molecular interaction between the cyclic nucleotide-binding homology domain and the eag domain of the hERG channelen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1016/j.febslet.2014.05.056


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