 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](mn5017fig1mag.jpg)
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Figure 1
Sequence alignment and structural characterization of the mSTING and hSTING monomers. (a) Alignment of the C-terminal domain sequences of the mSTING and hSTING proteins. Invisible residues at the N-terminal and C-terminal ends are connected by dotted lines. Conserved residues are shown in red text. Secondary-structural elements (arrows, β-strands; tubes, α-helices) are shown above the mSTING sequence. The π-helix between the α5 and α6 helices is coloured magenta with highlighted residues. Residues involved in interaction with interfacial c-di-GMP are marked by red dots, while those interacting with peripheral c-di-GMP are marked by purple dots, except for residues Tyr166 and Phe278, which form hydrophobic stacks with guanine bases and are marked by blue dots. Residues that were invisible before peripheral c-di-GMP binding are connected by a dotted red line above the sequence. Clustered altered residues that lead to a loss of c-di-GMP binding capability (Burdette et al., 2011  ) are connected by horizontal brackets with altered residues marked by vertical lines. Two crucial residues, Ile199 and Tyr313, responsible for inducing IFN-β production are involved in forming a stable hydrophobic core and are highlighted in grey. Some hydrophobic residues that interact with Ile199 or Tyr313 are boxed in grey. (b) Stereoview of the superimposition of the mSTING (shown as a red cartoon) and hSTING (shown as a grey cartoon) monomeric structures. The β2–β3 and β5–α9 loops are invisible in hSTING and are circled by red and blue dotted lines, respectively, while the α7–α8 loop is invisible in mSTING and is circled by a green dotted line. |
![[Figure 1]](mn5017fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
