1ypq
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602601 602601]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 28: | Line 28: | ||
[[Category: Boyington, J C.]] | [[Category: Boyington, J C.]] | ||
[[Category: Park, H.]] | [[Category: Park, H.]] | ||
| - | [[Category: DIO]] | ||
[[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'' |
Revision as of 22:17, 30 March 2008
| |||||||
| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1YPU, 1YPO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Human Oxidized Low Density Lipoprotein Receptor LOX-1 Dioxane Complex
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.
About this Structure
1YPQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1., Park H, Adsit FG, Boyington JC, J Biol Chem. 2005 Apr 8;280(14):13593-9. Epub 2005 Feb 5. PMID:15695803
Page seeded by OCA on Mon Mar 31 01:17:05 2008
