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Figure 2.
Figure 2. Overall Structure of Sec17Two ribbon drawings of
Sec17 related by a 180° rotation around the long axis of the
protein. The nine N-terminal α helices form a twisted sheet
that gives rise to two faces and two ridges. The five C-terminal
α helices form a more globular bundle, which is
asymmetrically disposed with respect to the N-terminal sheet,
creating a significant cleft on one face of the molecule.
Residues colored red and yellow correspond, respectively, to
inhibitory and noninhibitory peptides from an earlier study
([15]).
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