1pqc
From Proteopedia
(New page: 200px<br /> <applet load="1pqc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pqc, resolution 2.80Å" /> '''HUMAN LXR BETA HORM...) |
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| - | [[Image:1pqc.gif|left|200px]]<br /> | + | [[Image:1pqc.gif|left|200px]]<br /><applet load="1pqc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1pqc" size=" | + | |
caption="1pqc, resolution 2.80Å" /> | caption="1pqc, resolution 2.80Å" /> | ||
'''HUMAN LXR BETA HORMONE RECEPTOR COMPLEXED WITH T0901317'''<br /> | '''HUMAN LXR BETA HORMONE RECEPTOR COMPLEXED WITH T0901317'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of the liver X receptor LXRbeta (NR1H2) have been | + | The structures of the liver X receptor LXRbeta (NR1H2) have been determined in complexes with two synthetic ligands, T0901317 and GW3965, to 2.1 and 2.4 A, respectively. Together with its isoform LXRalpha (NR1H3) it regulates target genes involved in metabolism and transport of cholesterol and fatty acids. The two LXRbeta structures reveal a flexible ligand-binding pocket that can adjust to accommodate fundamentally different ligands. The ligand-binding pocket is hydrophobic but with polar or charged residues at the two ends of the cavity. T0901317 takes advantage of this by binding to His-435 close to H12 while GW3965 orients itself with its charged group in the opposite direction. Both ligands induce a fixed "agonist conformation" of helix H12 (also called the AF-2 domain), resulting in a transcriptionally active receptor. |
==About this Structure== | ==About this Structure== | ||
| - | 1PQC 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 444 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PQC 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=444:'>444</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Carlquist, M.]] | [[Category: Carlquist, M.]] | ||
[[Category: Farnegardh, M.]] | [[Category: Farnegardh, M.]] | ||
| - | [[Category: Gustafsson, J | + | [[Category: Gustafsson, J A.]] |
[[Category: Ljunggren, J.]] | [[Category: Ljunggren, J.]] | ||
[[Category: Sun, S.]] | [[Category: Sun, S.]] | ||
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[[Category: lxrb+t0901317]] | [[Category: lxrb+t0901317]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:28 2008'' |
Revision as of 12:31, 21 February 2008
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HUMAN LXR BETA HORMONE RECEPTOR COMPLEXED WITH T0901317
Overview
The structures of the liver X receptor LXRbeta (NR1H2) have been determined in complexes with two synthetic ligands, T0901317 and GW3965, to 2.1 and 2.4 A, respectively. Together with its isoform LXRalpha (NR1H3) it regulates target genes involved in metabolism and transport of cholesterol and fatty acids. The two LXRbeta structures reveal a flexible ligand-binding pocket that can adjust to accommodate fundamentally different ligands. The ligand-binding pocket is hydrophobic but with polar or charged residues at the two ends of the cavity. T0901317 takes advantage of this by binding to His-435 close to H12 while GW3965 orients itself with its charged group in the opposite direction. Both ligands induce a fixed "agonist conformation" of helix H12 (also called the AF-2 domain), resulting in a transcriptionally active receptor.
About this Structure
1PQC is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the liver X receptor beta reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands., Farnegardh M, Bonn T, Sun S, Ljunggren J, Ahola H, Wilhelmsson A, Gustafsson JA, Carlquist M, J Biol Chem. 2003 Oct 3;278(40):38821-8. Epub 2003 Jun 20. PMID:12819202
Page seeded by OCA on Thu Feb 21 14:31:28 2008
