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Fig. 5. Homology models of the structural constraints in jShak1 based on the
crystal structure of RatKV1.2. (A)Overlay of S3 and S4 showing the
extremely short three amino acid S3-S4 linker which anchors the C-terminal end
of S3 closely to the N-terminal end of S4 in jShak1 during gating transitions.
The homology model of jShak1 (blue) is placed over the model of
RatKV1.2 (gold). The basic residues in S4 are illustrated as
side-chain sticks, and transmembrane helices are labelled. (B)Overlay of the
highly conserved S4-S5 linker (L4-5) that is conserved in both
RatKV1.2 (gold) and jShak1 (blue). The L4-5 linker couples the
translocation of the voltage sensor to the opening of activation gate. This
conserved mechanism suggests that length insertions in the short S4 of
jShak1 should move residues extracellularly rather than modify the
amphipathic packing of L4-5.
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