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. 2013 Jun 17;110(27):10940–10945. doi: 10.1073/pnas.1300686110

Fig. 2.

Fig. 2.

The C-terminal “propeptide” harbors a death domain like fold. (A) Prolegumain consists of a catalytic domain (green, Val18-Met286), an AP (blue, Lys287–Asn323), and a LSAM domain (wheat, Asp324–Tyr433). Cleavages at the α- (KRK289) and β-sites (N323D324) release the AP and, thus, renders the active site (C189) accessible. (B) Topology diagram of LSAM (colored in wheat) compared with classical death domains (colored in red).

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