1f2i: Difference between revisions

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-[[Image:1f2i.gif|left|200px]]
- {{Structure
+==COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA==
-|PDB= 1f2i |SIZE=350|CAPTION= <scene name='initialview01'>1f2i</scene>, resolution 2.35&Aring;
+<StructureSection load='1f2i' size='340' side='right'caption='[[1f2i]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
+<table><tr><td colspan='2'>[[1f2i]] is a 12 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=1F2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2I FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
-|GENE= GENE FOR ZIF12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
+<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=1f2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2i OCA], [https://pdbe.org/1f2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2i RCSB], [https://www.ebi.ac.uk/pdbsum/1f2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2i ProSAT]</span></td></tr>
+</table>
-'''COCRYSTAL STRUCTURE OF SELECTED ZINC FINGER DIMER BOUND TO DNA'''
+== 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.
+== Evolutionary Conservation ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-Protein-protein interactions often play a crucial role in stabilizing protein-DNA complexes and thus facilitate site-specific DNA recognition. We have worked to incorporate such protein-protein contacts into our design and selection strategies for short peptide extensions that promote cooperative binding of zinc finger proteins to DNA. We have determined the crystal structure of one of these fusion protein-DNA complexes. The selected peptide extension was found to mediate dimerization by reaching across the dyad axis and contacting a hydrophobic patch on the surface of the zinc finger bound to the adjacent DNA site. The peptide-zinc finger protein interactions observed in this structure are similar to those of some homeodomain heterodimers. We also find that the region of the zinc finger surface contacted by the selected peptide extension corresponds to surfaces that also make key interactions in the zinc finger proteins GLI and SWI5.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/1f2i_consurf.spt"</scriptWhenChecked>
-F2I is a [[Single protein]] structure of sequence 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=1F2I OCA].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-Selected peptide extension contacts hydrophobic patch on neighboring zinc finger and mediates dimerization on DNA., Wang BS, Grant RA, Pabo CO, Nat Struct Biol. 2001 Jul;8(7):589-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11427887 11427887]
+</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=1f2i ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Grant RA]]
-[[Category: Grant, R A.]]
+[[Category: Pabo CO]]
-[[Category: Pabo, C O.]]
+[[Category: Wang BS]]
-[[Category: Wang, B S.]]
-[[Category: ZN]]
-[[Category: cooperativity]]
-[[Category: dimer]]
-[[Category: protein-dna complex]]
-[[Category: zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:29 2008''