Overview
- The Rockefeller University team reports the findings in Nature Communications, presenting a native-like view of the human receptor complex on December 16.
- In resting conditions the complex appears compact and closed, then extends in a jack-in-the-box motion upon antigen–HLA engagement to initiate signaling.
- Detergent-based preparations used in prior structural studies likely stripped stabilizing lipids and left the complex artificially open, obscuring the transition.
- Researchers reconstituted the full eight-protein complex into lipid nanodiscs and imaged it by cryo-EM, a technically demanding approach that preserved key membrane interactions.
- The structural mechanism suggests ways to tune activation thresholds in engineered receptors and may inform vaccine antigen selection, with further functional validation still required.