2i13

<StructureSection load='2i13' size='340' side='right' caption='[[2i13]], [[Resolution|resolution]] 1.96&Aring;' scene=''>

<table><tr><td colspan='2'>[[2i13]] is a 6 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=2I13 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I13 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=2i13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i13 OCA], [http://pdbe.org/2i13 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i13 RCSB], [http://www.ebi.ac.uk/pdbsum/2i13 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/ZSCA2_MOUSE ZSCA2_MOUSE]] May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/2i13_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 ==

Cys2-His2 zinc fingers are one of the most common types of DNA-binding domains. Modifications to zinc-finger binding specificity have recently enabled custom DNA-binding proteins to be designed to a wide array of target sequences. We present here a 1.96 A structure of Aart, a designed six-zinc finger protein, bound to a consensus DNA target site. This is the first structure of a designed protein with six fingers, and was intended to provide insights into the unusual affinity and specificity characteristics of this protein. Most protein-DNA contacts were found to be consistent with expectations, while others were unanticipated or insufficient to explain specificity. Several were unexpectedly mediated by glycerol, water molecules or amino acid-base stacking interactions. These results challenge some conventional concepts of recognition, particularly the finding that triplets containing 5'A, C, or T are typically not specified by direct interaction with the amino acid in position 6 of the recognition helix.

Structure of Aart, a designed six-finger zinc finger peptide, bound to DNA.,Segal DJ, Crotty JW, Bhakta MS, Barbas CF 3rd, Horton NC J Mol Biol. 2006 Oct 20;363(2):405-21. Epub 2006 Aug 11. PMID:16963084<ref>PMID:16963084</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 2i13" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Bhakta, M]]

[[Category: Horton, N C]]

[[Category: III, C F.Barbas]]

[[Category: Segal, D J]]

[[Category: Dna binding]]

[[Category: Dna binding protein-dna complex]]

[[Category: Zinc finger]]