1a1h

<StructureSection load='1a1h' size='340' side='right' caption='[[1a1h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1a1h]] is a 3 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=1A1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A1H FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[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://pdbe.org/1a1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a1h RCSB], [http://www.ebi.ac.uk/pdbsum/1a1h PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/1a1h_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

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.

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:9562555<ref>PMID:9562555</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1a1h" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Benson, T E]]

[[Category: Elrod-Erickson, M]]

[[Category: Pabo, C O]]

[[Category: Dna-binding protein]]

[[Category: Transcription-dna complex]]

[[Category: Zinc finger]]