1bgf: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 ==STAT-4 N-DOMAIN==
-<StructureSection load='1bgf' size='340' side='right' caption='[[1bgf]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+<StructureSection load='1bgf' size='340' side='right'caption='[[1bgf]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bgf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BGF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bgf]] is a 1 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=1BGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BGF FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgf OCA], [http://pdbe.org/1bgf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bgf RCSB], [http://www.ebi.ac.uk/pdbsum/1bgf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgf 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]] 1.45&#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=1bgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgf OCA], [https://pdbe.org/1bgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bgf RCSB], [https://www.ebi.ac.uk/pdbsum/1bgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/STAT4_MOUSE STAT4_MOUSE]] Carries out a dual function: signal transduction and activation of transcription.
+[https://www.uniprot.org/uniprot/STAT4_MOUSE STAT4_MOUSE] Carries out a dual function: signal transduction and activation of transcription.
 == 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/bg/1bgf_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/1bgf_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 18: / Line 19: @@
 </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=1bgf ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-STATs (signal transducers and activators of transcription) are a family of transcription factors that are specifically activated to regulate gene transcription when cells encounter cytokines and growth factors. The crystal structure of an NH2-terminal conserved domain (N-domain) comprising the first 123 residues of STAT-4 was determined at 1.45 angstroms. The domain consists of eight helices that are assembled into a hook-like structure. The N-domain has been implicated in several protein-protein interactions affecting transcription, and it enables dimerized STAT molecules to polymerize and to bind DNA cooperatively. The structure shows that N-domains can interact through an extensive interface formed by polar interactions across one face of the hook. Mutagenesis of an invariant tryptophan residue at the heart of this interface abolished cooperative DNA binding by the full-length protein in vitro and reduced the transcriptional response after cytokine stimulation in vivo.
-Structure of the amino-terminal protein interaction domain of STAT-4.,Vinkemeier U, Moarefi I, Darnell JE Jr, Kuriyan J Science. 1998 Feb 13;279(5353):1048-52. PMID:9461439<ref>PMID:9461439</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1bgf" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Darnell, J E]]
+[[Category: Mus musculus]]
-[[Category: Kuriyan, J]]
+[[Category: Darnell JE]]
-[[Category: Moarefi, I]]
+[[Category: Kuriyan J]]
-[[Category: Vinkemeier, U]]
+[[Category: Moarefi I]]
-[[Category: Dna-binding]]
+[[Category: Vinkemeier U]]
-[[Category: Regulation]]
-[[Category: Transcription factor]]