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Figure 1.
Comparison of WSK3 with KcsA. (A and B) The averaged NMR
structure (green in A) and the 20 lowest energy structures
(black in B) of WSK3 are superimposed on the low-K^+ KcsA
crystal structure (1K4D in light gray). In A, the mutations made
to facilitate water solubility and agitoxin-2 binding are
highlighted in orange and black, respectively. (C) Sequence
alignment and relative numbering of KcsA and WSK3. The mutations
are highlighted in gold. The selectivity filter is enclosed in
the red rectangle. The kink near V85 in WSK3 is marked with an
asterisk. The underlined residues are non-α-helix in some
structures.
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