1yxk: Difference between revisions

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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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1yxk, resolution 2.40Å" />

'''Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) disulfide-linked dimer'''<br />

==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.

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==

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==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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1YXK OCA].

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==

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[[Category: scavenger receptor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:26:~~15 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:06 2008''

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@@ Line 1: / Line 1: @@
-[[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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1yxk, resolution 2.40&Aring;" />
 '''Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) disulfide-linked dimer'''<br />
 ==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.
+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==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-YXK 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YXK OCA].
+YXK 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==
@@ Line 35: / Line 34: @@
 [[Category: scavenger receptor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:26:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:06 2008''