1yxj

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(New page: 200px<br /> <applet load="1yxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yxj, resolution 1.78&Aring;" /> '''Crystal structure o...)
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<applet load="1yxj" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) at low pH'''<br />
'''Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) at low pH'''<br />
==Overview==
==Overview==
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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.
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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==
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1YXJ 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 EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YXJ OCA].
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1YXJ 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=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YXJ OCA].
==Reference==
==Reference==
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[[Category: scavenger receptor]]
[[Category: scavenger receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:26:12 2007''
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''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

Image:1yxj.gif

1yxj, resolution 1.78Å

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Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) at low pH

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

1YXJ is a Single protein structure of sequence from Homo sapiens with as ligand. 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

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