1yxk
From Proteopedia
(New page: 200px<br /> <applet load="1yxk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yxk, resolution 2.40Å" /> '''Crystal structure o...) |
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| - | [[Image:1yxk.gif|left|200px]]<br /> | + | [[Image:1yxk.gif|left|200px]]<br /><applet load="1yxk" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yxk" size=" | + | |
caption="1yxk, resolution 2.40Å" /> | caption="1yxk, resolution 2.40Å" /> | ||
'''Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) disulfide-linked dimer'''<br /> | '''Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) disulfide-linked dimer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is | + | Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the "basic spine," consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1YXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: scavenger receptor]] | [[Category: scavenger receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:06 2008'' |
Revision as of 14:10, 21 February 2008
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Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) disulfide-linked dimer
Contents |
Overview
Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the "basic spine," consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed.
Disease
Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[602601]
About this Structure
1YXK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL., Ohki I, Ishigaki T, Oyama T, Matsunaga S, Xie Q, Ohnishi-Kameyama M, Murata T, Tsuchiya D, Machida S, Morikawa K, Tate S, Structure. 2005 Jun;13(6):905-17. PMID:15939022
Page seeded by OCA on Thu Feb 21 16:10:06 2008
Categories: Homo sapiens | Single protein | Ishigaki, T. | Machida, S. | Matsunaga, S. | Morikawa, K. | Murata, T. | Ohki, I. | Ohnishi-Kameyama, M. | Oyama, T. | Tate, S. | Tsuchiya, D. | Xie, Q. | C-type lectin-like domain | Ctld | Lox-1 | Nk cell receptor | Oxidized ldl receptor | Scavenger receptor
