2adr: Difference between revisions
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<StructureSection load='2adr' size='340' side='right' caption='[[2adr]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | <StructureSection load='2adr' size='340' side='right' caption='[[2adr]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2adr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2adr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ADR 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> | </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=2adr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2adr RCSB], [http://www.ebi.ac.uk/pdbsum/2adr 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=2adr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adr OCA], [http://pdbe.org/2adr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2adr RCSB], [http://www.ebi.ac.uk/pdbsum/2adr PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2adr" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 18824]] | ||
[[Category: Bowers, P M]] | [[Category: Bowers, P M]] | ||
[[Category: Kleivt, R E]] | [[Category: Kleivt, R E]] |
Revision as of 01:05, 12 September 2015
ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURESADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES
Structural highlights
Function[ADR1_YEAST] Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2). 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 PubMedThe region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site. We have used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms a compact domain consisting of three antiparallel strands that contact A-T base pairs in the major groove. The three-strand domain is a novel fold among all known DNA-binding proteins. The PAR shares sequence homology with the N-terminal regions of other zinc finger proteins, suggesting that it represents a new DNA-binding module that extends the binding repertoire of zinc finger proteins. A folding transition and novel zinc finger accessory domain in the transcription factor ADR1.,Bowers PM, Schaufler LE, Klevit RE Nat Struct Biol. 1999 May;6(5):478-85. PMID:10331877[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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