1an2

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{{Seed}}
 
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[[Image:1an2.png|left|200px]]
 
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==RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1an2", creates the "Structure Box" on the page.
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<StructureSection load='1an2' size='340' side='right'caption='[[1an2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1an2| PDB=1an2 | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1an2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_8479534}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1an2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 8479534 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8479534}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Homo sapiens]]
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1AN2 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA].
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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==Reference==
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[[Category: Burley SK]]
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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]
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[[Category: Ferre-D'Amare AR]]
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[[Category: Single protein]]
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[[Category: Prendergast GC]]
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[[Category: Amare, A R.Ferre-D.]]
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[[Category: Ziff EB]]
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[[Category: Burley, S K.]]
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[[Category: Prendergast, G C.]]
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[[Category: Ziff, E B.]]
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[[Category: Double helix]]
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[[Category: Protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:11:54 2008''
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Current revision

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

PDB ID 1an2

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