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...
Main Authors: | , , , , |
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Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-01-01
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Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4500599?pdf=render |