1n7d: Difference between revisions
New page: left|200px<br /> <applet load="1n7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n7d, resolution 3.70Å" /> '''Extracellular domai... |
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[[Image:1n7d.gif|left|200px]]<br /> | [[Image:1n7d.gif|left|200px]]<br /><applet load="1n7d" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1n7d, resolution 3.70Å" /> | caption="1n7d, resolution 3.70Å" /> | ||
'''Extracellular domain of the LDL receptor'''<br /> | '''Extracellular domain of the LDL receptor'''<br /> | ||
==Overview== | ==Overview== | ||
The low-density lipoprotein receptor mediates cholesterol homeostasis | The low-density lipoprotein receptor mediates cholesterol homeostasis through endocytosis of lipoproteins. It discharges its ligand in the endosome at pH < 6. In the crystal structure at pH = 5.3, the ligand-binding domain (modules R2 to R7) folds back as an arc over the epidermal growth factor precursor homology domain (the modules A, B, beta propeller, and C). The modules R4 and R5, which are critical for lipoprotein binding, associate with the beta propeller via their calcium-binding loop. We propose a mechanism for lipoprotein release in the endosome whereby the beta propeller functions as an alternate substrate for the ligand-binding domain, binding in a calcium-dependent way and promoting lipoprotein release. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1N7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and KEG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1N7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=KEG:'>KEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7D OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brown, M | [[Category: Brown, M S.]] | ||
[[Category: Deisenhofer, J.]] | [[Category: Deisenhofer, J.]] | ||
[[Category: Goldstein, J | [[Category: Goldstein, J L.]] | ||
[[Category: Henderson, K.]] | [[Category: Henderson, K.]] | ||
[[Category: Henry, L.]] | [[Category: Henry, L.]] | ||
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[[Category: ldl-receptor]] | [[Category: ldl-receptor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:04 2008'' |
Revision as of 15:03, 21 February 2008
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Extracellular domain of the LDL receptor
OverviewOverview
The low-density lipoprotein receptor mediates cholesterol homeostasis through endocytosis of lipoproteins. It discharges its ligand in the endosome at pH < 6. In the crystal structure at pH = 5.3, the ligand-binding domain (modules R2 to R7) folds back as an arc over the epidermal growth factor precursor homology domain (the modules A, B, beta propeller, and C). The modules R4 and R5, which are critical for lipoprotein binding, associate with the beta propeller via their calcium-binding loop. We propose a mechanism for lipoprotein release in the endosome whereby the beta propeller functions as an alternate substrate for the ligand-binding domain, binding in a calcium-dependent way and promoting lipoprotein release.
DiseaseDisease
Known disease associated with this structure: Hypercholesterolemia, familial OMIM:[606945]
About this StructureAbout this Structure
1N7D is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the LDL receptor extracellular domain at endosomal pH., Rudenko G, Henry L, Henderson K, Ichtchenko K, Brown MS, Goldstein JL, Deisenhofer J, Science. 2002 Dec 20;298(5602):2353-8. Epub 2002 Nov 29. PMID:12459547
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