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Figure 1.
Figure 1. Structure of α-cat 82–279(A) Topology diagram
of the α-cat 82–279 fold. Helices are shown as cylinders and
are numbered consecutively; residue numbers at the beginning and
the end of the helices are indicated. The region colored in red
represents the dimerization interface.(B) Ribbon diagram of
α-cat 82–279 protomer structure. Two different views related
by a 180° rotation about the horizontal axis are shown.
Proline residues in helices 3 and 4 are shown in red. This
figure, and Figure 1 and Figure 5, were made with MOLSCRIPT (
[26]).(C) Ribbon diagram of the α-cat 82–279 dimer.
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