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1a1h

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QGSR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a1h"

Categories: Large Structures | Mus musculus | Benson TE | Elrod-Erickson M | Pabo CO

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-[[Image:1a1h.jpg|left|200px]]
- {{Structure
+==QGSR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)==
-|PDB= 1a1h |SIZE=350|CAPTION= <scene name='initialview01'>1a1h</scene>, resolution 1.600&Aring;
+<StructureSection load='1a1h' size='340' side='right'caption='[[1a1h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+<table><tr><td colspan='2'>[[1a1h]] is a 3 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=1A1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A1H 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]] 1.6&#8491;</td></tr>
-|GENE=
+<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>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a1h OCA], [https://pdbe.org/1a1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a1h RCSB], [https://www.ebi.ac.uk/pdbsum/1a1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a1h ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a1h OCA], [http://www.ebi.ac.uk/pdbsum/1a1h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a1h RCSB]</span>
+== 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 ==
-'''QGSR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/1a1h_consurf.spt"</scriptWhenChecked>
-BACKGROUND: Zinc fingers of the Cys2-His2 class comprise one of the largest families of eukaryotic DNA-binding motifs and recognize a diverse set of DNA sequences. These proteins have a relatively simple modular structure and key base contacts are typically made by a few residues from each finger. These features make the zinc finger motif an attractive system for designing novel DNA-binding proteins and for exploring fundamental principles of protein-DNA recognition. RESULTS: Here we report the X-ray crystal structures of zinc finger-DNA complexes involving three variants of Zif268, with multiple changes in the recognition helix of finger one. We describe the structure of each of these three-finger peptides bound to its corresponding target site. To help elucidate the differential basis for site-specific recognition, the structures of four other complexes containing various combinations of these peptides with alternative binding sites have also been determined. CONCLUSIONS: The protein-DNA contacts observed in these complexes reveal the basis for the specificity demonstrated by these Zif268 variants. Many, but not all, of the contacts can be rationalized in terms of a recognition code, but the predictive value of such a code is limited. The structures illustrate how modest changes in the docking arrangement accommodate the new sidechain-base and sidechain-phosphate interactions. Such adaptations help explain the versatility of naturally occurring zinc finger proteins and their utility in design.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-A1H 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=1A1H OCA].
+</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=1a1h ConSurf].
+<div style="clear:both"></div>
-==Reference==
+__TOC__
-High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition., Elrod-Erickson M, Benson TE, Pabo CO, Structure. 1998 Apr 15;6(4):451-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9562555 9562555]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Benson TE]]
-[[Category: Benson, T E.]]
+[[Category: Elrod-Erickson M]]
-[[Category: Elrod-Erickson, M.]]
+[[Category: Pabo CO]]
-[[Category: Pabo, C O.]]
-[[Category: complex (zinc finger/dna)]]
-[[Category: dna-binding protein]]
-[[Category: zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:07 2008''

1a1h

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QGSR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)

Structural highlights

Function

Evolutionary Conservation

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