1p47

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{{Seed}}
 
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[[Image:1p47.png|left|200px]]
 
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==Crystal Structure of tandem Zif268 molecules complexed to DNA==
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The line below this paragraph, containing "STRUCTURE_1p47", creates the "Structure Box" on the page.
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<StructureSection load='1p47' size='340' side='right'caption='[[1p47]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1p47]] is a 4 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=1P47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P47 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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{{STRUCTURE_1p47| PDB=1p47 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p47 OCA], [https://pdbe.org/1p47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p47 RCSB], [https://www.ebi.ac.uk/pdbsum/1p47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p47 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/1p47_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1p47 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Zinc-finger proteins offer a versatile and effective framework for the recognition of DNA binding sites. By connecting multiple fingers together with canonical TGEKP linkers, a protein may be designed to recognize almost any desired target DNA sequence. However, proteins containing more than three zinc-fingers do not bind as tightly as one might predict, and it appears that some type of strain is introduced when a six-finger protein is constructed with canonical linkers. In an attempt to understand the sources of this strain, we have solved the 2.2A resolution X-ray crystallographic structure of a complex that has two copies of the three-finger Zif268 protein bound to adjacent sites on one duplex DNA. Conceptually, this is equivalent to a six-finger protein in which the central linker has been removed and the complex has been allowed to "relax" to its most stable conformation. As in other Zif268-DNA complexes, the DNA is approximately linear and is slightly underwound. Surprisingly, the structure of the complex is similar (within 0.5A) to an arrangement that would allow a canonical linker at the center of the complex, and it seems possible that entropic effects (involving the librational degrees of freedom in the complex) could be important in determining optimal linker length.
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===Crystal Structure of tandem Zif268 molecules complexed to DNA===
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Constraints for zinc finger linker design as inferred from X-ray crystal structure of tandem Zif268-DNA complexes.,Peisach E, Pabo CO J Mol Biol. 2003 Jun 27;330(1):1-7. PMID:12818197<ref>PMID:12818197</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12818197}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1p47" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12818197 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12818197}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1P47 is a 4 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=1P47 OCA].
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==Reference==
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<ref group="xtra">PMID:12818197</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Pabo, C O.]]
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[[Category: Pabo CO]]
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[[Category: Peisach, E.]]
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[[Category: Peisach E]]
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[[Category: Dna-binding protein]]
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[[Category: Zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:31:40 2009''
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Current revision

Crystal Structure of tandem Zif268 molecules complexed to DNA

PDB ID 1p47

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