3dju: Difference between revisions

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-{{Seed}}
-[[Image:3dju.png|left|200px]]
-<!--
+==Crystal structure of human BTG2==
-The line below this paragraph, containing "STRUCTURE_3dju", creates the "Structure Box" on the page.
+<StructureSection load='3dju' size='340' side='right'caption='[[3dju]], [[Resolution|resolution]] 2.26&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'>[[3dju]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DJU 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]] 2.26&#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=3dju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dju OCA], [https://pdbe.org/3dju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dju RCSB], [https://www.ebi.ac.uk/pdbsum/3dju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dju ProSAT]</span></td></tr>
-{{STRUCTURE_3dju|  PDB=3dju  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BTG2_HUMAN BTG2_HUMAN] Involved in cell cycle regulation. Could be involved in the growth arrest and differentiation of the neuronal precursors (By similarity). Anti-proliferative protein. Modulates transcription regulation mediated by ESR1. Involved in mitochondrial depolarization and neurite outgrowth.<ref>PMID:12771185</ref> <ref>PMID:15788397</ref> <ref>PMID:18773938</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/dj/3dju_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=3dju ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BTG2 is the prototypical member of the TOB family and is known to be involved in cell growth, differentiation and DNA repair. As a transcriptional co-regulator, BTG2 interacts with CCR4-associated factor 1 (CAF1) and POP2 (CALIF), which are key components of the general CCR4/NOT multi-subunit transcription complex, and which are reported to play distinct roles as nucleases involved in mRNA deadenylation. Here we report the crystal structures of human BTG2 and mouse TIS21 to 2.3 A and 2.2 A resolution, respectively. The structures reveal the putative CAF1 binding site. CAF1 deadenylase assays were performed with wild-type BTG2 and mutants that disrupt the interaction with CAF1. The results reveal the suppressive role of BTG2 in the regulation of CAF1 deadenylase activity. Our study provides insights into the formation of the BTG2-CAF1 complex and the potential role of BTG2 in the regulation of CAF1.
-===Crystal structure of human BTG2===
+Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity.,Yang X, Morita M, Wang H, Suzuki T, Yang W, Luo Y, Zhao C, Yu Y, Bartlam M, Yamamoto T, Rao Z Nucleic Acids Res. 2008 Dec;36(21):6872-81. Epub 2008 Oct 30. PMID:18974182<ref>PMID:18974182</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_18974182}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3dju" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 18974182 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18974182}}
+__TOC__
+</StructureSection>
-==About this Structure==
-DJU is a [[Single protein]] 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=3DJU OCA].
-==Reference==
-Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity., Yang X, Morita M, Wang H, Suzuki T, Yang W, Luo Y, Zhao C, Yu Y, Bartlam M, Yamamoto T, Rao Z, Nucleic Acids Res. 2008 Oct 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18974182 18974182]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
+[[Category: Bartlam M]]
-[[Category: Helix-turn-helix]]
+[[Category: Morita M]]
-[[Category: Transcription]]
+[[Category: Suzuki T]]
-[[Category: Transcription regulation]]
+[[Category: Wang H]]
+[[Category: Yamamoto T]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 10 20:13:17 2008''
+[[Category: Yang X]]