Structure and function in rhodopsin: the role of asparagine-linked glycosylation.

@article{Kaushal1994StructureAF,
  title={Structure and function in rhodopsin: the role of asparagine-linked glycosylation.},
  author={S Kaushal and Kevin D Ridge and Har Gobind Khorana},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 9},
  pages={4024-8}
}
Rhodopsin, the dim light photoreceptor of the rod cell, is an integral membrane protein that is glycosylated at Asn-2 and Asn-15. Here we report experiments on the role of the glycosylation in rhodopsin folding and function. Nonglycosylated opsin was prepared by expression of a wild-type bovine opsin gene in COS-1 cells in the presence of tunicamycin, an inhibitor of asparagine-linked glycosylation. The non-glycosylated opsin folded correctly as shown by its normal palmitoylation, transport to… CONTINUE READING

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