3f27: Difference between revisions

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-{{Seed}}
-[[Image:3f27.png|left|200px]]
-<!--
+==Structure of Sox17 Bound to DNA==
-The line below this paragraph, containing "STRUCTURE_3f27", creates the "Structure Box" on the page.
+<StructureSection load='3f27' size='340' side='right'caption='[[3f27]], [[Resolution|resolution]] 2.75&Aring;' 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'>[[3f27]] is a 3 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=3F27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F27 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">X-ray diffraction, [[Resolution|Resolution]] 2.75&#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=3f27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f27 OCA], [https://pdbe.org/3f27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f27 RCSB], [https://www.ebi.ac.uk/pdbsum/3f27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f27 ProSAT]</span></td></tr>
-{{STRUCTURE_3f27|  PDB=3f27  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SOX17_MOUSE SOX17_MOUSE] Acts as transcription regulator that binds target promoter DNA and bends the DNA. Binds to the sequences 5'-AACAAT-'3 or 5'-AACAAAG-3'. Modulates transcriptional regulation via WNT3A. Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays a key role in the regulation of embryonic development. Required for normal looping of the embryonic heart tube. Required for normal development of the definitive gut endoderm. Probable transcriptional activator in the premeiotic germ cells. Isoform 2 (T-SOX17) shows no DNA-binding activity.<ref>PMID:20802155</ref>
+== 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/f2/3f27_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=3f27 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Sox17 regulates endodermal lineage commitment and is thought to function antagonistically to the pluripotency determinant Sox2. To investigate the biochemical basis for the distinct functions of Sox2 and Sox17, we solved the crystal structure of the high mobility group domain of Sox17 bound to a DNA element derived from the Lama1 enhancer using crystals diffracting to 2.7 A resolution. Sox17 targets the minor groove and bends the DNA by approximately 80 degrees . The DNA architecture closely resembles the one seen for Sox2/DNA structures, suggesting that the degree of bending is conserved between both proteins and nucleotide substitutions have only marginal effects on the bending topology. Accordingly, affinities of Sox2 and Sox17 for the Lama1 element were found to be identical. However, when the Oct1 contact interface of Sox2 is compared with the corresponding region of Sox17, a significantly altered charge distribution is observed, suggesting differential co-factor recruitment that may explain their biological distinctiveness.
-===Structure of Sox17 Bound to DNA===
+The structure of Sox17 bound to DNA reveals a conserved bending topology but selective protein interaction platforms.,Palasingam P, Jauch R, Ng CK, Kolatkar PR J Mol Biol. 2009 May 8;388(3):619-30. Epub 2009 Mar 25. PMID:19328208<ref>PMID:19328208</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_19328208}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3f27" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19328208 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19328208}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-F27 is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F27 OCA].
-==Reference==
-<ref group="xtra">PMID:19328208</ref><references group="xtra"/>
 [[Category: Mus musculus]]
-[[Category: Jauch, R.]]
+[[Category: Jauch R]]
-[[Category: Kolatkar, P R.]]
+[[Category: Kolatkar PR]]
-[[Category: Ng, C K.L.]]
+[[Category: Ng CKL]]
-[[Category: Palasingam, P.]]
+[[Category: Palasingam P]]
-[[Category: Activator]]
-[[Category: Alternative splicing]]
-[[Category: Dna-binding]]
-[[Category: Endodermal]]
-[[Category: Hmg domain]]
-[[Category: Nucleus]]
-[[Category: Protein-dna complex]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Transcription/dna complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 29 20:53:44 2009''