==RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN==

<StructureSection load='1an2' size='340' side='right'caption='[[1an2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>

<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://pdbe.org/1an2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1an2 RCSB], [http://www.ebi.ac.uk/pdbsum/1an2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1an2 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/MAX_HUMAN 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.

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== Publication Abstract from PubMed ==

The 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<ref>PMID:8479534</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Amare, A R.Ferre-D]]

[[Category: Transcription-dna complex]]