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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Bibliographic Details
Main Authors: Juan Martínez-Oliván, Hugo Fraga, Xabier Arias-Moreno, Salvador Ventura, Javier Sancho
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4500599?pdf=render