2i13: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i13]] is a 6 chain structure with 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=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> | <table><tr><td colspan='2'>[[2i13]] is a 6 chain structure with 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=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><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='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><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://www.rcsb.org/pdb/explore.do?structureId=2i13 RCSB], [http://www.ebi.ac.uk/pdbsum/2i13 PDBsum]</span></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://www.rcsb.org/pdb/explore.do?structureId=2i13 RCSB], [http://www.ebi.ac.uk/pdbsum/2i13 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://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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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Bhakta, M | [[Category: Bhakta, M]] | ||
[[Category: Crotty, J W | [[Category: Crotty, J W]] | ||
[[Category: Horton, N C | [[Category: Horton, N C]] | ||
[[Category: III, C F.Barbas | [[Category: III, C F.Barbas]] | ||
[[Category: Segal, D J | [[Category: Segal, D J]] | ||
[[Category: Dna binding]] | [[Category: Dna binding]] | ||
[[Category: Dna binding protein-dna complex]] | [[Category: Dna binding protein-dna complex]] | ||
[[Category: Zinc finger]] | [[Category: Zinc finger]] | ||
Revision as of 18:14, 25 December 2014
Aart, a six finger zinc finger designed to recognize ANN tripletsAart, a six finger zinc finger designed to recognize ANN triplets
Structural highlights
Function[ZSCA2_MOUSE] May be involved in transcriptional regulation during the post-meiotic stages of spermatogenesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCys2-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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