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Figure 1.
Figure 1. Structure of the (a) monomer and (b) dimer of
SARS-CoV Mpro. (a) Domains I (light blue) and II (green) each
contain a six-stranded b-barrel and domain III (orange) is
composed mainly of a-helices. The amino and the carboxy terminus
are marked by a blue and an orange sphere, respectively. The
flexible loops L1, L2, and L3 (red) comprise residues 138-145
(the oxyanion-binding loop), 165-172, and 185-200, respectively.
(b) a-Helices are red and b-strands are light blue. The amino
and the carboxy termini are marked by blue and orange spheres,
respectively. Dimerization is mainly due to interactions between
the helical domains III of each monomer (top). (c)
Superimposition (in stereo) of the C^a backbone as determined in
three different crystal forms. Blue, monoclinic form; red,
tetragonal form; green, orthorhombic form. (a) and (b) were
prepared by MOLSCRIPT,40 (c) was prepared by PyMOL.41
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