2i13: Difference between revisions

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<StructureSection load='2i13' size='340' side='right'caption='[[2i13]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
<StructureSection load='2i13' size='340' side='right'caption='[[2i13]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2i13]] is a 6 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2I13 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2i13]] is a 6 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=2I13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I13 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=2i13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i13 OCA], [https://pdbe.org/2i13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i13 RCSB], [https://www.ebi.ac.uk/pdbsum/2i13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i13 ProSAT]</span></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=2i13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i13 OCA], [https://pdbe.org/2i13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i13 RCSB], [https://www.ebi.ac.uk/pdbsum/2i13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i13 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ZSCA2_MOUSE ZSCA2_MOUSE]] May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis.  
[https://www.uniprot.org/uniprot/ZSCA2_MOUSE ZSCA2_MOUSE] May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2i13 ConSurf].
</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=2i13 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 2i13" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Bhakta, M]]
[[Category: Barbas III CF]]
[[Category: Crotty, J W]]
[[Category: Bhakta M]]
[[Category: Horton, N C]]
[[Category: Crotty JW]]
[[Category: III, C F.Barbas]]
[[Category: Horton NC]]
[[Category: Segal, D J]]
[[Category: Segal DJ]]
[[Category: Dna binding]]
[[Category: Dna binding protein-dna complex]]
[[Category: Zinc finger]]

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