View source for 1fjl


==HOMEODOMAIN FROM THE DROSOPHILA PAIRED PROTEIN BOUND TO A DNA OLIGONUCLEOTIDE==
<StructureSection load='1fjl' size='340' side='right'caption='[[1fjl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fjl]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FJL FirstGlance]. <br>
</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=1fjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjl OCA], [http://pdbe.org/1fjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fjl RCSB], [http://www.ebi.ac.uk/pdbsum/1fjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjl ProSAT]</span></td></tr>
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== Function ==
[[http://www.uniprot.org/uniprot/PRD_DROME PRD_DROME]] Pair-rule protein expressed in a segmentally repeating pattern to define the polarity of embryonic segments. Capable of sequence-specific DNA-binding. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fjl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fjl ConSurf].
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== Publication Abstract from PubMed ==
The crystal structure of the paired homeodomain bound to DNA as a cooperative dimer has been determined to 2.0 A resolution. Direct contacts between each homeodomain and the DNA are similar to those described previously. In addition, an extensive network of water molecules mediates contacts between the recognition helix and the DNA major groove. Several symmetrical contacts between the two homeodomains underlie the cooperative interaction, and deformations in the DNA structure are necessary for the establishment of these contacts. Comparison with structures of homeodomains bound monomerically to DNA suggests that the binding of a single paired homeodomain can introduce these DNA distortions, thus preparing a template for the cooperative interaction with a second homeodomain. This study shows how the paired (Pax) class homeodomains have achieved cooperativity in DNA binding without the assistance of other domains, thereby enabling the recognition of target sequences that are long enough to ensure specificity.

High resolution crystal structure of a paired (Pax) class cooperative homeodomain dimer on DNA.,Wilson DS, Guenther B, Desplan C, Kuriyan J Cell. 1995 Sep 8;82(5):709-19. PMID:7671301<ref>PMID:7671301</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 1fjl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drome]]
[[Category: Large Structures]]
[[Category: Desplan, C]]
[[Category: Guenther, B]]
[[Category: Kuriyan, J]]
[[Category: Wilson, D S]]
[[Category: Dna]]
[[Category: Dna-binding protein]]
[[Category: Paired box]]
[[Category: Transcription regulation]]
[[Category: Transcription-dna complex]]