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Figure 3.
Figure 3. View of the molecular surface of hTRX illustrating
the cleft in which the NFκB peptide is located. The degree of
curvature of the molecular surface is color coded from white
(convex) to dark gray (concave). Hence the cleft is visualized
as the contiguous boot-shaped gray region on the surface of
hTRX. The backbone of the peptide is shown in green, and side
chains are colored as follows: Phe, Tyr, Val, Pro and Cys in
yellow; Arg and His in blue; Glu in red and Ser in magenta. Note
that the side chains of Phe56 and His67 of the bound NFκB
peptide are disordered in solution. Figure 3. View of the
molecular surface of hTRX illustrating the cleft in which the
NFκB peptide is located. The degree of curvature of the
molecular surface is color coded from white (convex) to dark
gray (concave). Hence the cleft is visualized as the contiguous
boot-shaped gray region on the surface of hTRX. The backbone of
the peptide is shown in green, and side chains are colored as
follows: Phe, Tyr, Val, Pro and Cys in yellow; Arg and His in
blue; Glu in red and Ser in magenta. Note that the side chains
of Phe56 and His67 of the bound NFκB peptide are disordered in
solution. (Figure generated with the program GRASP [[3]83].)
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