1an2: Difference between revisions

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[[Image:1an2.gif|left|200px]]


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==RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN==
The line below this paragraph, containing "STRUCTURE_1an2", creates the "Structure Box" on the page.
<StructureSection load='1an2' size='340' side='right'caption='[[1an2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1an2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1AN2 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
-->
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1an2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an2 OCA], [https://pdbe.org/1an2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1an2 RCSB], [https://www.ebi.ac.uk/pdbsum/1an2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1an2 ProSAT]</span></td></tr>
{{STRUCTURE_1an2|  PDB=1an2  |  SCENE= }}
</table>
 
== Function ==
'''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''
[https://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.
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
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.
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1an2_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1AN2 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</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=1an2 ConSurf].
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:[http://www.ncbi.nlm.nih.gov/pubmed/8479534 8479534]
<div style="clear:both"></div>
[[Category: Single protein]]
__TOC__
[[Category: Amare, A R.Ferre-D.]]
</StructureSection>
[[Category: Burley, S K.]]
[[Category: Homo sapiens]]
[[Category: Prendergast, G C.]]
[[Category: Large Structures]]
[[Category: Ziff, E B.]]
[[Category: Mus musculus]]
[[Category: Double helix]]
[[Category: Burley SK]]
[[Category: Protein-dna complex]]
[[Category: Ferre-D'Amare AR]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:28:10 2008''
[[Category: Prendergast GC]]
[[Category: Ziff EB]]

Latest revision as of 09:32, 7 February 2024

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

1an2 is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

1an2, resolution 2.90Å

Drag the structure with the mouse to rotate

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OCA
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