LDL receptor

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
<StructureSection load='2w2m' size='350' side='right' caption='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]])' scene=''>
<StructureSection load='2w2m' size='350' side='right' caption='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]])' scene=''>
 +
== Function ==
 +
'''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 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<ref>PMID:19299327</ref>.
-
'''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.
+
== Structural highlights ==
 +
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.
</StructureSection>
</StructureSection>
Line 53: Line 56:
**[[3p5b]], [[3p5c]] – hLDLR EGFP, oligosaccharide-rich, domains + proprotein convertase subtilisin/kexin 9<br />
**[[3p5b]], [[3p5c]] – hLDLR EGFP, oligosaccharide-rich, domains + proprotein convertase subtilisin/kexin 9<br />
}}
}}
 +
== References ==
 +
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:54, 10 April 2016

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)

Drag the structure with the mouse to rotate

3D structures of LDL receptor

Updated on 10-April-2016

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/LDL_receptor"
Personal tools