Ontology highlight
ABSTRACT:
SUBMITTER: Huang S
PROVIDER: S-EPMC2803231 | biostudies-literature | 2010 Feb
REPOSITORIES: biostudies-literature
Huang Sha S Henry Lisa L Ho Yiu Kee YK Pownall Henry J HJ Rudenko Gabby G
Journal of lipid research 20090811 2
The LDL receptor (LDL-R) mediates cholesterol metabolism in humans by binding and internalizing cholesterol transported by LDL. Several different molecular mechanisms have been proposed for the binding of LDL to LDL-R at neutral plasma pH and for its release at acidic endosomal pH. The crystal structure of LDL-R at acidic pH shows that the receptor folds back on itself in a closed form, obscuring parts of the ligand binding domain with the epidermal growth factor (EGF)-precursor homology domain. ...[more]