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Figure 2 | Molecular Cancer

Figure 2

From: Tissue Inhibitor of Metalloproteinases-4. The road less traveled

Figure 2

Cartoon representation of the crystallography structure of the human TIMP-2 in uncomplexed state (A) and the bovine TIMP-2 complexed with the catalytic domain on the metalloproteinase 13 (cdMMP-13) (B). The regions of TIMP-2 folded as helices and β-strands are colored in red and yellow, respectively. The six conserved disulfide bridges characterizing the TIMP structure are shown in blue in figure A. In B, the cdMMP-13 is colored in blue and the catalytic Zn is colored in magenta and shown in space-filled format. The residues Cys1, Ser2 and Cys3 that form the core of the molecular edge of the inhibitor that occupies the active-site cleft of the MMP, and the Cys72 and Cys101 are shown in stick format and colored yellow. The figure was prepared using PyMOL® and the coordinates of PDB 1BR9 (Fig. 2A) and PDB 2E2D (Fig. 2B).

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