Skip to main content
. 2024 Jan 25;33(9):752–767. doi: 10.1093/hmg/ddae005

Figure 2.

Figure 2

The residues involved in the SCSD-associated SPINT2 mutations are not in the reactive site of the Kunitz domain 2. (A) The 3D structure of HAI-2 Kunitz domain 2 was built using the AlphaFold protein structure database and Swiss-PdbViewer 4.10. The P1 site ARG143 (shown in red) and the four residues that are found to be mutated in SCSD patients, including Arg-148 (R148 in blue), Phe-161 (F161 in yellow), Tyr-163 (Y163 in green) and Gly-168 (G168 in light purple), are indicated. (B) The schematic 2D structure of HAI-2 Kunitz domain 2 is presented using single letter amino acid notation. The two β strands are indicated in yellow, one α helix in blue, and the three pairs of disulfide bonds as C1-C6, C2-C4, and C3-C5. The amino acid residues mutated in SCSD patients are indicated in red circle and the mutations are also indicated as R148C, R148H, F161C, Y163C, and G168S in red).