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TitleA Cryptic Pocket Allosterically Modulates Oligosaccharide Binding to DC-SIGN.
Journal, issue, pagesJACS Au, Vol. 6, Issue 2, Page 1048-1060, Year 2026
Publish dateFeb 23, 2026
AuthorsJonathan Lefèbre / Maurice Besch / Marcelo Daniel Gamarra / Jan-Oliver Kapp-Joswig / Annika Balke / Stevan Aleksić / Henry Flatau / Gregor Suchy / Elena Georgieva / Patrick Scheerer / Bettina G Keller / Carlos Pablo Modenutti / Christoph Rademacher /
PubMed AbstractDC-SIGN is a C-type lectin receptor expressed on antigen-presenting cells that is crucial for pathogen recognition and immune modulation. Here, we identify and characterize a previously unrecognized ...DC-SIGN is a C-type lectin receptor expressed on antigen-presenting cells that is crucial for pathogen recognition and immune modulation. Here, we identify and characterize a previously unrecognized cryptic allosteric pocket in DC-SIGN using molecular dynamics simulations, NMR spectroscopy, cryogenic electron microscopy, and biochemical assays. Rotation of the gatekeeper residue M270 exposes the pocket whose occupancy modulates glycan binding. Mutations M270F and T314A mimic the occupied and unoccupied states of this pocket, respectively, shifting the conformational equilibrium of α-helix 2 and altering the oligosaccharide affinity via the extended carbohydrate binding site. While Ca coordination at the canonical binding site remains unaffected, our data reveal a complex interplay between the Ca binding sites and the canonical and extended glycan binding surfaces. These findings uncover a hierarchical allosteric mechanism that enables selective tuning of glycan affinity and suggest the cryptic pocket as a novel target for drug discovery in C-type lectins.
External linksJACS Au / PubMed:41755834 / PubMed Central
MethodsEM (single particle)
Resolution7.6 Å
Structure data

EMDB-56237: Cryo-EM structure of the extracellular domain of DC-SIGN
Method: EM (single particle) / Resolution: 7.6 Å

Source
  • Homo sapiens (human)

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