1ajj: Difference between revisions
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|PDB= 1ajj |SIZE=350|CAPTION= <scene name='initialview01'>1ajj</scene>, resolution 1.7Å | |PDB= 1ajj |SIZE=350|CAPTION= <scene name='initialview01'>1ajj</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ajj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ajj OCA], [http://www.ebi.ac.uk/pdbsum/1ajj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ajj RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The low-density lipoprotein receptor (LDLR) is responsible for the uptake of cholesterol-containing lipoprotein particles into cells. The amino-terminal region of LDLR, which consists of seven tandemly repeated, approximately 40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins. LDL-A modules are biologically ubiquitous domains, found in over 100 proteins in the sequence database. The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 A resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules. Naturally occurring point mutations found in patients with the disease familial hypercholesterolaemia alter residues that directly coordinate Ca2+ or that serve as scaffolding residues of LR5. | The low-density lipoprotein receptor (LDLR) is responsible for the uptake of cholesterol-containing lipoprotein particles into cells. The amino-terminal region of LDLR, which consists of seven tandemly repeated, approximately 40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins. LDL-A modules are biologically ubiquitous domains, found in over 100 proteins in the sequence database. The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 A resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules. Naturally occurring point mutations found in patients with the disease familial hypercholesterolaemia alter residues that directly coordinate Ca2+ or that serve as scaffolding residues of LR5. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Fass, D.]] | [[Category: Fass, D.]] | ||
[[Category: Kim, P S.]] | [[Category: Kim, P S.]] | ||
[[Category: calcium]] | [[Category: calcium]] | ||
[[Category: cysteine-rich module]] | [[Category: cysteine-rich module]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:41:34 2008'' | ||
