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Figure 1.
Figure 1. Molecular Structure of K^b and Location of the
Mutations in K^bm1 and K^bm8(A) Ribbon diagram of wild-type K^b
with peptide (magenta) bound in an extended conformation within
the binding groove formed by the α helices and the β sheet
floor.(B) Mutated side chains in K^bm1 and K^bm8 are shown in
green and orange, respectively, while wild-type side chains are
shown in (A).(C) Superimposed Cα tracings of the α[1]α[2]
helices of K^b-VSV8 (yellow), K^b-SEV9 (blue), K^bm1-VSV8
(magenta), K^bm1-SEV9 (red), K^bm8-VSV8 (cyan), and K^bm8-SEV9
(green). Peptide-contacting side chains from the helices, some
of which have different conformations in the six complexes, are
shown
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