File:4F5W.pse: Difference between revisions

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The 4F5W structure captures STING in its calm, inactive state. In this form, the protein sits as an open dimer, with the two arms of the molecule gently spread apart. Because no ligand is bound, STING isn’t under any pressure to change shape—so it sta
 
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Latest revision as of 17:50, 30 November 2025

The 4F5W structure captures STING in its calm, inactive state. In this form, the protein sits as an open dimer, with the two arms of the molecule gently spread apart. Because no ligand is bound, STING isn’t under any pressure to change shape—so it stays relaxed. The C-terminal tail remains neatly tucked away, almost like a safety lock that keeps the protein from accidentally activating.

This structure represents STING exactly as it looks before sensing any danger, making it the perfect reference for understanding how the protein later closes, shifts, and comes alive when cGAMP or other ligands bind.

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current17:50, 30 November 2025 (518 KB)Disha Sonwani (talk | contribs)
17:21, 30 November 2025 (518 KB)Disha Sonwani (talk | contribs)The 4F5W structure captures STING in its calm, inactive state. In this form, the protein sits as an open dimer, with the two arms of the molecule gently spread apart. Because no ligand is bound, STING isn’t under any pressure to change shape, so it stay
17:20, 30 November 2025 (518 KB)Disha Sonwani (talk | contribs)The 4F5W structure captures STING in its calm, inactive state. In this form, the protein sits as an open dimer, with the two arms of the molecule gently spread apart. Because no ligand is bound, STING isn’t under any pressure to change shape—so it sta

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Proteopedia Page Contributors and Editors (what is this?)

Disha Sonwani