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Article

Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants.

Proceedings of the National Academy of Sciences of the United States of America - 24 Apr 2001

Hwa J, Klein-Seetharaman J, Khorana H G

Abstract excerpt

Retinitis pigmentosa (RP) point mutations in both the intradiscal (ID) and transmembrane domains of rhodopsin cause partial or complete misfolding of rhodopsin, resulting in loss of 11-cis-retinal binding. Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin. Here we report on direct...

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Identifiers

PMID: 11320236
DOI: 10.1073/pnas.061632798
PMCID: PMC33130

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Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants.PMID 11320236Read ↗

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