LDL receptor (LDLR) mediates the endocytosis of cholesterol-rich LDL. LDLR recognizes the apoprotein B100 which is embedded in the outer layer of the LDL particle. LDLR consist of a ligand-binding domain (LBD residues 1-292), epidermal growth factor precursor homology domain (EGFP residues 293-699), oligosaccharide-rich domain (residues 700-758), membrane-spanning domain (residues 759-781) and cytoplasmic domain (residues 782-832). LDLR LBD contains 7 ca. 40 amino acid long repeats (LB) containing 6 cysteine residues, making a calcium binding octahedral structure. LDLR EGFP contains 2 EGF repeats followed by 6 YWTD repeats and another EGF repeat. LDLR sits on the cell surface and binds LDL particles which circulate in the blood stream. LDLR transports the LDL particle into the cell where the cholesterol is used. Upon release of the LDL particle, the LDLR is recycled back into the cell membrane surface.
3D structures of LDL receptor
Updated on 08-May-2013
hLDLR LBD
1ldl – hLDLR LBD LB1 - human - NMR
1ldr – hLDLR LBD LB2 - NMR
1ajj – hLDLR LBD LB5
1d2j, 1f8z – hLDLR LBD LB6 - NMR
1f5y – hLDLR LBD LB1,LB2 - NMR
2lgp – hLDLR LBD LB4,LB5 - NMR
1xfe – hLDLR LBD LB7,EGF - NMR
hLDLR LBD complex with protein
2fcw – hLDLR LBD LB3,LB4 + α-2-macroglobulin receptor-associated protein
2kri – hLDLR LBD LB4 + β-2-glycoprotein - NMR
hLDLR EGFP
1ijq – hLDLR YWTD-EGF
1hj7 – hLDLR EGF-EGF - NMR
1hz8, 1i0u – hLDLR EGF1, EGF2 - NMR
hLDLR EGFP complex with protein
3bps, 2w2m, 2w2o, 2w2p, 2w2q, 3gcx – hLDLR EGF1, EGF2 + proprotein convertase subtilisin/kexin 9
2w2n, 3gcw – hLDLR EGF1, EGF2 (mutant) + proprotein convertase subtilisin/kexin 9
hLDLR cytoplasmic domain
3so6 – hLDLR cytoplasmic domain C terminal + LDLR adaptor protein
hLDLR several domains
1n7d – hLDLR LBD,EGFP domains
3m0c – hLDLR LBD,EGFP, oligosaccharide-rich, membrane-spanning domains + proprotein convertase subtilisin/kexin 9
3p5b, 3p5c – hLDLR EGFP, oligosaccharide-rich, domains + proprotein convertase subtilisin/kexin 9
