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. Author manuscript; available in PMC: 2017 Aug 11.
Published in final edited form as: Biochem Biophys Res Commun. 2016 Jan 30;471(1):103–108. doi: 10.1016/j.bbrc.2016.01.172

Figure 2.

Figure 2

Comparison of the structures of SPINK2, 6, and 7. (A) Sequence alignment of SPINK2, 6, and 7. The position of residues known to bind to the active site of the proteases is marked by an arrow. (B) Superposition of the averaged structures of SPINK6 (green), SPINK2 (yellow, PDB ID: 2jxd) and SPINK7 (blue, PDB ID: 2leo). For superposition the secondary structure elements were used. Side chains of the residues known to bind to the active site of the S1-pocket of the proteases are depicted and labeled. (C) Structural ensembles of SPINK6, SPINK7 and SPINK2 (from left to right). In all three molecules, the N-terminal region, which contains the amino-acid residue side chain involved in the inhibition of KLKs, exhibits a high flexibility. Molecules are shown in the orientation with respect to the central helix.