Search

Your search keyword '"Bulleid, N."' showing total 4 results
Start Over Author "Bulleid, N." Publisher wiley
4 results on '"Bulleid, N."'

4. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha

Author

Roberto Sitia, Ineke Braakman, Adam M. Benham, A. Cabibbo, Anna Fassio, Neil J. Bulleid, Benham, A. M., Cabibbo, A., Fassio, A., Bulleid, N. J., Sitia, Roberto, and Braakman, I.

Subjects
Protein Folding, Glycosylation, Protein Conformation, Stereochemistry, CHO Cells, HIV Envelope Protein gp120, Endoplasmic Reticulum, General Biochemistry, Genetics and Molecular Biology, Protein structure, ER oxidoreductin, Cricetinae, Animals, Humans, Amino Acid Sequence, Disulfides, Protein disulfide-isomerase, Molecular Biology, chemistry.chemical_classification, Membrane Glycoproteins, General Immunology and Microbiology, biology, General Neuroscience, Endoplasmic reticulum, Active site, Articles, chemistry, Biochemistry, biology.protein, Protein folding, Oxidoreductases, Glycoprotein, Oxidation-Reduction, HeLa Cells, Cysteine
Abstract

The presence of correctly formed disulfide bonds is crucial to the structure and function of proteins that are synthesized in the endoplasmic reticulum (ER). Disulfide bond formation occurs in the ER owing to the presence of several specialized catalysts and a suitable redox potential. Work in yeast has indicated that the ER resident glycoprotein Ero1p provides oxidizing equivalents to newly synthesized proteins via protein disulfide isomerase (PDI). Here we show that Ero1-Lalpha, the human homolog of Ero1p, exists as a collection of oxidized and reduced forms and covalently binds PDI. We analyzed Ero1-Lalpha cysteine mutants in the presumed active site C(391)VGCFKC(397). Our results demonstrate that this motif is important for protein folding, structural integrity, protein half-life and the stability of the Ero1-Lalpha-PDI complex.

Published
2000

Catalog

Books, media, physical & digital resources
See catalog results