4m4x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:24, 1 March 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4m4x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M4X FirstGlance]. <br>
<table><tr><td colspan='2'>[[4m4x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M4X FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4m4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4x OCA], [https://pdbe.org/4m4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m4x RCSB], [https://www.ebi.ac.uk/pdbsum/4m4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4x ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.551&#8491;</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4m4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4x OCA], [https://pdbe.org/4m4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m4x RCSB], [https://www.ebi.ac.uk/pdbsum/4m4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/AHR_MOUSE AHR_MOUSE] Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues.<ref>PMID:1314586</ref> <ref>PMID:7961644</ref> <ref>PMID:7969080</ref> <ref>PMID:8806883</ref> <ref>PMID:9427285</ref> <ref>PMID:10973493</ref> <ref>PMID:10639156</ref>
[https://www.uniprot.org/uniprot/AHR_MOUSE AHR_MOUSE] Ligand-activated transcriptional activator. Binds to the XRE promoter region of genes it activates. Activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Involved in cell-cycle regulation. Likely to play an important role in the development and maturation of many tissues.<ref>PMID:1314586</ref> <ref>PMID:7961644</ref> <ref>PMID:7969080</ref> <ref>PMID:8806883</ref> <ref>PMID:9427285</ref> <ref>PMID:10973493</ref> <ref>PMID:10639156</ref>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
The aryl hydrocarbon receptor (AHR) is a ligand-dependent transcription factor that binds to xenobiotics and responds by regulating the expression of gene programs required for detoxification and metabolism. AHR and its heterodimerization partner aryl hydrocarbon receptor nuclear translocator (ARNT) belong to the bHLH (basic helix-loop-helix)-PAS (PER-ARNT-SIM) family of transcription factors. Here we report the 2.55 A resolution crystal structure of the mouse AHR PAS-A domain, which represents the first AHR derived protein structure. The AHR PAS-A domain forms a helix-swapped homodimer in the crystal and also in solution. Through a detailed mutational analysis of all interface residues, we identified several hydrophobic residues that are important for the AHR dimerization and function. Our crystallographic visualization of the AHR PAS-A dimerization leads us to propose a mode of heterodimerization with ARNT that is supported by both biochemical and cell-based data. Our studies also highlight the residues of other mammalian bHLH-PAS proteins that are likely involved in their homo- or heterodimerization.
 
- 
-
Structure and Dimerization Properties of the Aryl Hydrocarbon Receptor (AHR) PAS-A Domain.,Wu D, Potluri N, Kim Y, Rastinejad F Mol Cell Biol. 2013 Sep 3. PMID:24001774<ref>PMID:24001774</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 4m4x" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>

Current revision

Structure and Dimerization Properties of the Aryl Hydrocarbon Receptor (AHR) PAS-A Domain

PDB ID 4m4x

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4m4x"
Personal tools