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Title: Misfolded opsin mutants display elevated β -sheet structure

Mutations in rhodopsin can cause misfolding and aggregation of the receptor, which leads to retinitis pigmentosa, a progressive retinal degenerative disease. The structure adopted by misfolded opsin mutants and the associated cell toxicity is poorly understood. Förster resonance energy transfer (FRET) and Fourier transform infrared (FTIR) microspectroscopy were utilized to probe within cells the structures formed by G188R and P23H opsins, which are misfolding mutants that cause autosomal dominant retinitis pigmentosa. Also, both mutants formed aggregates in the endoplasmic reticulum and exhibited altered secondary structure with elevated β-sheet and reduced α-helical content. The newly formed β-sheet structure may facilitate the aggregation of misfolded opsin mutants. In conclusion, the effects observed for the mutants were unrelated to retention of opsin molecules in the endoplasmic reticulum itself.
 [1] ;  [2] ;  [3] ;  [2]
  1. Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source-II
  2. Case Western Reserve University, Cleveland, OH (United States). Department of Ophthalmology and Visual Sciences and Department of Molecular Medicine, Cleveland Clinic Lerner College of Medicine
  3. Case Western Reserve University, Cleveland, OH (United States). Department of Ophthalmology and Visual Sciences
Publication Date:
Report Number(s):
Journal ID: ISSN 0014-5793
Grant/Contract Number:
SC00112704; AC02-98CH10886; AC02-05CH11231
Accepted Manuscript
Journal Name:
FEBS Letters
Additional Journal Information:
Journal Volume: 589; Journal Issue: 20PartB; Journal ID: ISSN 0014-5793
Federation of European Biochemical Societies
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; G protein-coupled receptor; Membrane protein; Protein aggregation; Protein misfolding; Secondary structure
OSTI Identifier: