ArticlebioRxiv : the preprint server for biology2026
Conformational signatures of native ligand and pharmacochaperone binding in rhodopsin.
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Rhodopsin misfolding underlies rhodopsin-linked retinitis pigmentosa, and small-molecule pharmacochaperones represent a promising therapeutic strategy. However, the mechanisms by which these compounds interact with and stabilize rhodopsin remain poorly understood. Here, we combine backbone amide hydrogen-deuterium exchange mass spectrometry (amide HDX-MS), histidine-specific HDX (His-HDX), protein structure network (PSN) analysis, molecular docking, and functional spectroscopy to define ligand-induced conformational signatures in this receptor elicited by three non-retinoid small molecules, quercetin, myricetin, and the chromenone CR5, and to compare them with those of the native chromophore 11-
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