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Biophys J 2007 Oct 01;937:2332-40. doi: 10.1529/biophysj.107.109702.
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Serial perturbation of MinK in IKs implies an alpha-helical transmembrane span traversing the channel corpus.

Chen H , Goldstein SA .

I(Ks) channels contain four pore-forming KCNQ1 subunits and two accessory MinK subunits. MinK influences surface expression, voltage-dependence of gating, conduction, and pharmacology to yield the attributes characteristic of native channels in heart. The structure and location of the MinK transmembrane domain (TMD) remains a matter of scrutiny. As perturbation of gating analysis has correctly inferred the peripheral location and alpha-helical nature of TMDs in pore-forming subunits, the method is applied here to human MinK. Tryptophan and Asparagine substitution at 23 consecutive sites yields perturbation with alpha-helical periodicity (residues 44-56) followed by an alternating impact pattern (residues 56-63). Arginine substitution across the span suggests that as few as eight sites are occluded from aqueous solution (residues 50-57). We favor a TMD model that is alpha-helical with the external portion of the span at a lipid-protein boundary and the inner portion within the channel corpus in complex interactions.

PubMed ID: 17545244
PMC ID: PMC1965433
Article link: Biophys J

Species referenced: Xenopus laevis
Genes referenced: kcne1 kcnq1 mink1 ttn

References [+] :
Abbott, MiRP1 forms IKr potassium channels with HERG and is associated with cardiac arrhythmia. 1999, Pubmed, Xenbase