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![[Figure 3]](ai5017fig3mag.jpg)
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Figure 3
Structure of hGSDMD-CTD–Peptide 2 and the conformational changes upon peptide binding. (a) Chemical structure of the cyclic Peptide 2. The S—S bond for peptide cyclization is highlighted in the red box. (b) Global structure of the hGSDMD–Peptide 2 complex. hGSDMD-CTD is colored pink and the peptide is in yellow. (c) Superposition of the hGSDMD-CTD–Peptide 2 complex structure (pink/yellow) with apo full-length hGSDMD (gray, PDB entry 6n9o). The N-terminus and C-terminus are labeled N′ and C′, respectively. 1271 atoms were aligned with an r.m.s.d. of 1.336 Å. (d) Superposition of the hGSDMD-CTD–Peptide 2 complex structure (pink) with apo hGSDMD-CTD (gray, PDB entry 5n1h). The area of observed conformational change for the hGSDMD structure is highlighted in the blue box. α-Helices are shown as cylinders. A close-up view of the hGSDMD conformational change at the interface. The hGSDMD-CTD–Peptide 2 complex is shown in blue and apo hGSDMD-CTD is in gray. (e) Overall structure of two adjacent hGSDMD-CTD–Peptide 2 complex molecules in the asymmetric unit displaying the binding interface of the two linearized peptides. The two hGSDMD-CTD molecules are colored pink and green, and the peptides are displayed in yellow and cyan, respectively. |
![[Figure 3]](ai5017fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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