LDL receptor

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'''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 LBD residues 133-273 are named C-type lectin-like domain. 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.
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'''LDL (Low Density Lipoprotein) 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 LBD residues 133-273 are named C-type lectin-like domain. 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.
</StructureSection>
</StructureSection>
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**[[2lgp]] – hLDLR LB4,LB5 - NMR<br />
**[[2lgp]] – hLDLR LB4,LB5 - NMR<br />
**[[1xfe]] – hLDLR LB7,EGF - NMR<br />
**[[1xfe]] – hLDLR LB7,EGF - NMR<br />
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**[[1yxj]], [[1yxk]] – hLDLR LBD LB4,LB5, LB6<br />
*hLDLR ligand-binding domain complex with protein
*hLDLR ligand-binding domain complex with protein
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**[[1hj7]] – hLDLR EGF-EGF - NMR<br />
**[[1hj7]] – hLDLR EGF-EGF - NMR<br />
**[[1hz8]], [[1i0u]] – hLDLR EGF1, EGF2 - NMR<br />
**[[1hz8]], [[1i0u]] – hLDLR EGF1, EGF2 - NMR<br />
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**[[2mg9]] – hLDLR EGF1 - NMR<br />
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**[[4ne9]] – hLDLR EGF1 + PCSK9<br />
*hLDLR EGFP complex with protein
*hLDLR EGFP complex with protein

Revision as of 09:00, 3 May 2015

Structure of human LDLR EGF precursor homology domain (magenta) complex with proprotein convertase subtilisin/kexin 9-CoA reductase (grey and green) and Ca+2 ions (PDB entry 2w2m)

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3D structures of LDL receptor

Updated on 03-May-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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