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Figure 1.
Fig. 1. Ribbon structure of human m-calpain in the
absence of calcium, shown in reference orientation. The 80-kDa
L-chain starts in the molecular center (green, dI), folds into
the surface of the dIIa subdomain (gold, I  II linker),
forms the papain-like left-side part of the catalytic domain dII
(gold, dIIa) and the right-side barrel-like subdomain dIIb
(red), descends through the open II III loop
(red), builds domain dIII (blue), runs down (magenta, III IV), and
forms the right-side calmodulin-like domain dIV (yellow). The
30-kDa S-chain becomes visible from Thr95S onwards (magenta, dV)
before forming the left-side calmodulin domain dVI (orange). The
catalytic residues Cys105L, His262L, and Asn286L together with
Trp106L, Pro287L, and Trp288L (top) are shown with all
non-hydrogen atoms. The figure was made with SETOR (34).
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