LDL receptor
From Proteopedia
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 receptorUpdated on 08-May-2013 hLDLR LBD1ldl – hLDLR LBD LB1 - human - NMR hLDLR LBD complex with protein2fcw – hLDLR LBD LB3,LB4 + α-2-macroglobulin receptor-associated protein hLDLR EGFP1ijq – hLDLR YWTD-EGF hLDLR EGFP complex with protein3bps, 2w2m, 2w2o, 2w2p, 2w2q, 3gcx – hLDLR EGF1, EGF2 + proprotein convertase subtilisin/kexin 9 hLDLR cytoplasmic domain3so6 – hLDLR cytoplasmic domain C terminal + LDLR adaptor protein hLDLR several domains1n7d – hLDLR LBD,EGFP domains | ||||||||||||

