1llm: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1llm.jpg|left|200px]]<br /><applet load="1llm" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1llm, resolution 1.50&Aring;" />
-'''Crystal Structure of a Zif23-GCN4 Chimera Bound to DNA'''<br />
-==Overview==
+==Crystal Structure of a Zif23-GCN4 Chimera Bound to DNA==
+<StructureSection load='1llm' size='340' side='right'caption='[[1llm]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1llm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLM FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1llm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llm OCA], [https://pdbe.org/1llm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llm RCSB], [https://www.ebi.ac.uk/pdbsum/1llm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EGR1_MOUSE EGR1_MOUSE] Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'(EGR-site). Activates the transcription of target genes whose products are required for mitogenesis and differentiation.[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
+== 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/ll/1llm_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=1llm ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
 Proteins that employ dimerization domains to bind cooperatively to DNA have a number of potential advantages over monomers with regards to gene regulation. Using a combination of structure-based design and phage display, a dimeric Cys(2)His(2) zinc finger protein has been created that binds cooperatively to DNA via an attached leucine zipper dimerization domain. This chimera, derived from components of Zif268 and GCN4, displayed excellent DNA-binding specificity, and we now report the 1.5 A resolution cocrystal structure of the Zif268-GCN4 homodimer bound to DNA. This structure shows how phage display has annealed the DNA binding and dimerization domains into a single functional unit. Moreover, this chimera provides a potential platform for the creation heterodimeric zinc finger proteins that can regulate a desired target gene through cooperative DNA recognition.
-==About this Structure==
+Structure of a designed dimeric zinc finger protein bound to DNA.,Wolfe SA, Grant RA, Pabo CO Biochemistry. 2003 Nov 25;42(46):13401-9. PMID:14621985<ref>PMID:14621985</ref>
-LLM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus_and_saccharomyces_cerevisiae Mus musculus and saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLM OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structure of a designed dimeric zinc finger protein bound to DNA., Wolfe SA, Grant RA, Pabo CO, Biochemistry. 2003 Nov 25;42(46):13401-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14621985 14621985]
+</div>
-[[Category: Mus musculus and saccharomyces cerevisiae]]
+<div class="pdbe-citations 1llm" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Grant, R A.]]
+<references/>
-[[Category: Pabo, C O.]]
+__TOC__
-[[Category: Wolfe, S A.]]
+</StructureSection>
-[[Category: ZN]]
+[[Category: Large Structures]]
-[[Category: dimerization]]
+[[Category: Mus musculus]]
-[[Category: dna recognition]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: leucine zipper]]
+[[Category: Grant RA]]
-[[Category: structure-based design]]
+[[Category: Pabo CO]]
-[[Category: x-ray crystallography]]
+[[Category: Wolfe SA]]
-[[Category: zinc fingers]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:09 2008''