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Nature Structural Biology  10, 153 - 154 (2003)
doi:10.1038/nsb0303-153

Co-translocational misfolding in the ER of living cells

Sheena E. Radford

Sheena E. Radford is in the School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK. s.e.radford@leeds.ac.uk

Recent experiments have shown that the co-translational folding of the multi-domain LDL receptor in the endoplasmic reticulum does not occur in a vectorial manner. Instead, newly translated chains form misfolded states involving incorrect disulfide bonds between residues distant in sequence.

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REFERENCE
Chaperones, Chaperonin and Heat-Shock Proteins
Nature Encyclopaedia of Life Sciences
Peptide Bonds, Disulfide Bonds and Properties of Small Peptides
Nature Encyclopaedia of Life Sciences

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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