1an2: Difference between revisions
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<StructureSection load='1an2' size='340' side='right' caption='[[1an2]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1an2' size='340' side='right' caption='[[1an2]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1an2]] is a 2 chain structure | <table><tr><td colspan='2'>[[1an2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AN2 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=1an2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1an2 RCSB], [http://www.ebi.ac.uk/pdbsum/1an2 PDBsum]</span></td></tr> | </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=1an2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an2 OCA], [http://pdbe.org/1an2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1an2 RCSB], [http://www.ebi.ac.uk/pdbsum/1an2 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 1an2" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Amare, A R.Ferre-D]] | [[Category: Amare, A R.Ferre-D]] | ||
[[Category: Burley, S K]] | [[Category: Burley, S K]] | ||
Revision as of 05:25, 10 September 2015
RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAINRECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN
Structural highlights
Function[MAX_HUMAN] Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. 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 three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain.,Ferre-D'Amare AR, Prendergast GC, Ziff EB, Burley SK Nature. 1993 May 6;363(6424):38-45. PMID:8479534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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