Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor

The LDL receptor internalizes circulating LDL and VLDL particles for degradation. Its extracellular binding domain contains ten (seven LA and three EGF) cysteine-rich modules, each bearing three disulfide bonds. Despite the enormous number of disulfide combinations possible, LDLR oxidative folding l...

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Detalles Bibliográficos
Autores principales: Martínez-Oliván, Juan, Fraga, Hugo, Arias-Moreno, Xabier, Ventura, Salvador, Sancho, Javier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4500599/
https://www.ncbi.nlm.nih.gov/pubmed/26168158
http://dx.doi.org/10.1371/journal.pone.0132141

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4500599/
https://www.ncbi.nlm.nih.gov/pubmed/26168158
http://dx.doi.org/10.1371/journal.pone.0132141

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