1ypq: Difference between revisions
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|PDB= 1ypq |SIZE=350|CAPTION= <scene name='initialview01'>1ypq</scene>, resolution 1.40Å | |PDB= 1ypq |SIZE=350|CAPTION= <scene name='initialview01'>1ypq</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=DIO:1,4-DIETHYLENE DIOXIDE'>DIO</scene> | |LIGAND= <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ypu|1YPU]], [[1ypo|1YPO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ypq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypq OCA], [http://www.ebi.ac.uk/pdbsum/1ypq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ypq RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
The lectin-like oxidized low density lipoprotein receptor-1 (Lox-1) mediates the recognition and internalization of oxidatively modified low density lipoprotein by vascular endothelial cells. This interaction results in a number of pro-atherogenic cellular responses that probably play a significant role in the pathology of atherosclerosis. The 1.4 angstrom crystal structure of the extracellular C-type lectin-like domain of human Lox-1 reveals a heart-shaped homodimer with a ridge of six basic amino acids extending diagonally across the apolar top of Lox-1, a central hydrophobic tunnel that extends through the entire molecule, and an electrostatically neutral patch of 12 charged residues that resides next to the tunnel at each opening. Based on the arrangement of critical binding residues on the Lox-1 structure, we propose a binding mode for the recognition of modified low density lipoprotein and other Lox-1 ligands. | The lectin-like oxidized low density lipoprotein receptor-1 (Lox-1) mediates the recognition and internalization of oxidatively modified low density lipoprotein by vascular endothelial cells. This interaction results in a number of pro-atherogenic cellular responses that probably play a significant role in the pathology of atherosclerosis. The 1.4 angstrom crystal structure of the extracellular C-type lectin-like domain of human Lox-1 reveals a heart-shaped homodimer with a ridge of six basic amino acids extending diagonally across the apolar top of Lox-1, a central hydrophobic tunnel that extends through the entire molecule, and an electrostatically neutral patch of 12 charged residues that resides next to the tunnel at each opening. Based on the arrangement of critical binding residues on the Lox-1 structure, we propose a binding mode for the recognition of modified low density lipoprotein and other Lox-1 ligands. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Boyington, J C.]] | [[Category: Boyington, J C.]] | ||
[[Category: Park, H.]] | [[Category: Park, H.]] | ||
[[Category: c-type lectin like domain]] | [[Category: c-type lectin like domain]] | ||
[[Category: lox-1,ctld]] | |||
[[Category: lox-1]] | |||
[[Category: nk cell receptor]] | [[Category: nk cell receptor]] | ||
[[Category: oxidized low density lipoprotein receptor]] | [[Category: oxidized low density lipoprotein receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:17:05 2008'' | ||