1xls: Difference between revisions

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[[Image:1xls.gif|left|200px]]<br />

[[Image:1xls.gif|left|200px]]<br /><applet load="1xls" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1xls" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1xls, resolution 2.96Å" />

'''Crystal structure of the mouse CAR/RXR LBD heterodimer bound to TCPOBOP and 9cRA and a TIF2 peptide containg the third LXXLL motifs'''<br />

==Overview==

Constitutive androstane receptor (CAR) induces xenobiotic, bilirubin, and, thyroid hormone metabolism as a heterodimer with the retinoid X receptor, (RXR). Unlike ligand-dependent nuclear receptors, CAR is constitutively, active. Here, we report the heterodimeric structure of the CAR and RXR, ligand binding domains (LBDs), which reveals an unusually large, dimerization interface and a small CAR ligand binding pocket. Constitutive, CAR activity appears to be mediated by the compact nature of the CAR LBD, that displays several unique features including a shortened AF2 helix and, helix H10, which are linked by a two-turn helix that normally adopts an, extended loop in other receptors, and an extended helix H2 that stabilizes, the canonical LBD fold by packing tightly against helix H3. These, structural observations provide a molecular framework for understanding, the atypical transcriptional activation properties of CAR.

Constitutive androstane receptor (CAR) induces xenobiotic, bilirubin, and thyroid hormone metabolism as a heterodimer with the retinoid X receptor (RXR). Unlike ligand-dependent nuclear receptors, CAR is constitutively active. Here, we report the heterodimeric structure of the CAR and RXR ligand binding domains (LBDs), which reveals an unusually large dimerization interface and a small CAR ligand binding pocket. Constitutive CAR activity appears to be mediated by the compact nature of the CAR LBD that displays several unique features including a shortened AF2 helix and helix H10, which are linked by a two-turn helix that normally adopts an extended loop in other receptors, and an extended helix H2 that stabilizes the canonical LBD fold by packing tightly against helix H3. These structural observations provide a molecular framework for understanding the atypical transcriptional activation properties of CAR.

==About this Structure==

1XLS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with REA and TCD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA].

1XLS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=REA:'>REA</scene> and <scene name='pdbligand=TCD:'>TCD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA].

==Reference==

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Line 14:

[[Category: Mus musculus]]

[[Category: Protein complex]]

[[Category: Cha, J.Y.]]

[[Category: Cha, J Y.]]

[[Category: Kliewer, S.A.]]

[[Category: Kliewer, S A.]]

[[Category: Li, Y.]]

[[Category: Repa, J.J.]]

[[Category: Repa, J J.]]

[[Category: Reynolds, R.]]

[[Category: Suino, K.]]

[[Category: Xu, H.E.]]

[[Category: Xu, H E.]]

[[Category: peng, L.]]

[[Category: REA]]

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[[Category: xenobiotic]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:07:~~12 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:21 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1xls.gif|left|200px]]<br />
+[[Image:1xls.gif|left|200px]]<br /><applet load="1xls" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1xls" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1xls, resolution 2.96&Aring;" />
 '''Crystal structure of the mouse CAR/RXR LBD heterodimer bound to TCPOBOP and 9cRA and a TIF2 peptide containg the third LXXLL motifs'''<br />
 ==Overview==
-Constitutive androstane receptor (CAR) induces xenobiotic, bilirubin, and, thyroid hormone metabolism as a heterodimer with the retinoid X receptor, (RXR). Unlike ligand-dependent nuclear receptors, CAR is constitutively, active. Here, we report the heterodimeric structure of the CAR and RXR, ligand binding domains (LBDs), which reveals an unusually large, dimerization interface and a small CAR ligand binding pocket. Constitutive, CAR activity appears to be mediated by the compact nature of the CAR LBD, that displays several unique features including a shortened AF2 helix and, helix H10, which are linked by a two-turn helix that normally adopts an, extended loop in other receptors, and an extended helix H2 that stabilizes, the canonical LBD fold by packing tightly against helix H3. These, structural observations provide a molecular framework for understanding, the atypical transcriptional activation properties of CAR.
+Constitutive androstane receptor (CAR) induces xenobiotic, bilirubin, and thyroid hormone metabolism as a heterodimer with the retinoid X receptor (RXR). Unlike ligand-dependent nuclear receptors, CAR is constitutively active. Here, we report the heterodimeric structure of the CAR and RXR ligand binding domains (LBDs), which reveals an unusually large dimerization interface and a small CAR ligand binding pocket. Constitutive CAR activity appears to be mediated by the compact nature of the CAR LBD that displays several unique features including a shortened AF2 helix and helix H10, which are linked by a two-turn helix that normally adopts an extended loop in other receptors, and an extended helix H2 that stabilizes the canonical LBD fold by packing tightly against helix H3. These structural observations provide a molecular framework for understanding the atypical transcriptional activation properties of CAR.
 ==About this Structure==
-XLS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with REA and TCD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA].
+XLS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=REA:'>REA</scene> and <scene name='pdbligand=TCD:'>TCD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XLS OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Cha, J.Y.]]
+[[Category: Cha, J Y.]]
-[[Category: Kliewer, S.A.]]
+[[Category: Kliewer, S A.]]
 [[Category: Li, Y.]]
-[[Category: Repa, J.J.]]
+[[Category: Repa, J J.]]
 [[Category: Reynolds, R.]]
 [[Category: Suino, K.]]
-[[Category: Xu, H.E.]]
+[[Category: Xu, H E.]]
 [[Category: peng, L.]]
 [[Category: REA]]
@@ Line 30: / Line 29: @@
 [[Category: xenobiotic]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:07:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:21 2008''