2k7s: Difference between revisions

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-{{Seed}}
-[[Image:2k7s.png|left|200px]]
-<!--
+==Human ARNT C-Terminal PAS Domain, 3 Residue IB slip==
-The line below this paragraph, containing "STRUCTURE_2k7s", creates the "Structure Box" on the page.
+<StructureSection load='2k7s' size='340' side='right'caption='[[2k7s]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2k7s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K7S FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2k7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k7s OCA], [https://pdbe.org/2k7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k7s RCSB], [https://www.ebi.ac.uk/pdbsum/2k7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k7s ProSAT]</span></td></tr>
-{{STRUCTURE_2k7s|  PDB=2k7s  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARNT_HUMAN ARNT_HUMAN] Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer with HIF1A or EPAS1/HIF2A functions as a transcriptional regulator of the adaptive response to hypoxia.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/2k7s_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k7s ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The aryl hydrocarbon receptor nuclear translocator (ARNT) is a basic helix-loop-helix Period/ARNT/Single-minded (bHLH-PAS) protein that controls various biological pathways as part of dimeric transcriptional regulator complexes with other bHLH-PAS proteins. The two PAS domains within ARNT, PAS-A and PAS-B, are essential for the formation of these complexes because they mediate protein-protein interactions via residues located on their beta-sheet surfaces. While investigating the importance of residues in ARNT PAS-B involved in these interactions, we uncovered a point mutation (Y456T) on the solvent-exposed beta-sheet surface that allowed this domain to interconvert with a second, stable conformation. Although both conformations are present in equivalent quantities in the Y456T mutant, this can be shifted almost completely to either end point by additional mutations. A high-resolution solution structure of a mutant ARNT PAS-B domain stabilized in the new conformation revealed a 3-residue slip in register and accompanying inversion of the central Ibeta-strand. We have demonstrated that the new conformation has &gt;100-fold lower in vitro affinity for its heterodimerization partner, hypoxia-inducible factor 2alpha PAS-B. We speculate that the pliability in beta-strand register is related to the flexibility required of ARNT to bind to several partners and, more broadly, to the abilities of some PAS domains to regulate their activities in response to small-molecule cofactors.
-===Human ARNT C-Terminal PAS Domain, 3 Residue IB slip===
+ARNT PAS-B has a fragile native state structure with an alternative beta-sheet register nearby in sequence space.,Evans MR, Card PB, Gardner KH Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2617-22. Epub 2009 Feb 5. PMID:19196990<ref>PMID:19196990</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2k7s" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19196990}}, adds the Publication Abstract to the page
+*[[Factor inhibiting HIF|Factor inhibiting HIF]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19196990 is the PubMed ID number.
+*[[3D structures of hypoxia-inducible factor|3D structures of hypoxia-inducible factor]]
--->
+== References ==
-{{ABSTRACT_PUBMED_19196990}}
+<references/>
+__TOC__
-==Disease==
+</StructureSection>
-Known disease associated with this structure: Leukemia, acute myeloblastic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=126110 126110]]
-==About this Structure==
-K7S is a 1 chain 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=2K7S OCA].
-==Reference==
-<ref group="xtra">PMID:19196990</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Card, P B.]]
+[[Category: Large Structures]]
-[[Category: Evans, M R.]]
+[[Category: Card PB]]
-[[Category: Gardner, K H.]]
+[[Category: Evans MR]]
-[[Category: Activator]]
+[[Category: Gardner KH]]
-[[Category: Alternative splicing]]
-[[Category: Arnt pas-b]]
-[[Category: Beta-strand slip]]
-[[Category: Dna-binding]]
-[[Category: Nucleus]]
-[[Category: Pas domain]]
-[[Category: Polymorphism]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 11 10:55:02 2009''