LDL receptor

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<scene name='54/545853/Cv/7'>Ligand-binding domain (LBD) and epidermal growth factor precursor homology domain (EGFP) of LDLR</scene>.
<scene name='54/545853/Cv/7'>Ligand-binding domain (LBD) and epidermal growth factor precursor homology domain (EGFP) of LDLR</scene>.
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LDLR consists 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 ((LB1 residues 20-67; LB2 residues 55-104; LB3 residues 105-143; LB4 residues 144-196; LB5 residues 196-232; LB6 residues 234-272) containing 6 cysteine residues, making a calcium binding octahedral structure. LDLR EGFP contains 2 EGF repeats followed by 6 <scene name='54/545853/Cv/8'>YWTD repeats</scene> and another EGF repeat. LDLR LBD residues 133-273 are named C-type lectin-like domain.
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LDLR consists 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 (LB1 residues 20-67; LB2 residues 55-104; LB3 residues 105-143; LB4 residues 144-196; LB5 residues 196-232; LB6 residues 234-272) containing 6 cysteine residues, making a calcium binding octahedral structure. LDLR EGFP contains 2 EGF repeats followed by 6 <scene name='54/545853/Cv/8'>YWTD repeats</scene> and another EGF repeat. LDLR LBD residues 133-273 are named C-type lectin-like domain.
</StructureSection>
</StructureSection>

Revision as of 09:07, 18 May 2021

Structure of human LDLR LBD and EGFP domains (magenta) complex with proprotein convertase subtilisin/kexin 9-CoA reductase (cyan and green) and Ca+2 ions (green) (PDB entry 3m0c)

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3D structures of LDL receptor

Updated on 18-May-2021

References

  1. ↑ Goldstein JL, Brown MS. The LDL receptor. Arterioscler Thromb Vasc Biol. 2009 Apr;29(4):431-8. doi:, 10.1161/ATVBAHA.108.179564. PMID:19299327 doi:http://dx.doi.org/10.1161/ATVBAHA.108.179564
  2. ↑ Mak YT, Pang CP, Tomlinson B, Zhang J, Chan YS, Mak TW, Masarei JR. Mutations in the low-density lipoprotein receptor gene in Chinese familial hypercholesterolemia patients. Arterioscler Thromb Vasc Biol. 1998 Oct;18(10):1600-5. PMID:9763532

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