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Fig. 6 | Molecular Medicine

Fig. 6

From: Degradation of C1-Inhibitor by Plasmin: Implications for the Control of Inflammatory Processes

Fig. 6

Models of C1-Inh cleavage sites

(A) The homology-modeled serpin fold is denoted as a ribbon on which all 37 α-carbon atoms of Lys and Arg residues appear as blue and green spheres. The structure is viewed in the same orientation as Fig. 2 of Perkins (16). On the right, the 10 green spheres correspond to the proteolysis sites listed in Table 1, as identified by residue labeling. On the left, three orange spheres indicate the α-carbon atoms of Glu 117, Cys 182, and Cys 406 which define the location of the major glycosylated N-terminal extension of C1-Inh relative to the serpin fold (16). The location of three yellow spheres indicates the positions of glycosylation sites at Asn 216, Asn 231, and Asn 330. (B) The peptide released by cleavage between Gly 195 and Lys284 is marked in yellow while that between Lys 285 and Lys 359 is marked in purple. The structure is viewed at the same orientation as in A above. In (A) and (B), the reactive site loop in a helical conformation is located at the far right of the model as shown.

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