1an2: Difference between revisions

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-[[Image:1an2.gif|left|200px]]
- {{Structure
+==RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN==
-|PDB= 1an2 |SIZE=350|CAPTION= <scene name='initialview01'>1an2</scene>, resolution 2.900&Aring;
+<StructureSection load='1an2' size='340' side='right'caption='[[1an2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE=
+<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>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<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.ebi.ac.uk/pdbsum/1an2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1an2 RCSB]</span>
+[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]]
-'''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1an2_consurf.spt"</scriptWhenChecked>
-==Overview==
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-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.
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
-==About this Structure==
+</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].
-AN2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA].
+<div style="clear:both"></div>
+__TOC__
-==Reference==
+</StructureSection>
-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]
+[[Category: Homo sapiens]]
-[[Category: ]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Mus musculus]]
-[[Category: Amare, A R.Ferre-D.]]
+[[Category: Burley SK]]
-[[Category: Burley, S K.]]
+[[Category: Ferre-D'Amare AR]]
-[[Category: Prendergast, G C.]]
+[[Category: Prendergast GC]]
-[[Category: Ziff, E B.]]
+[[Category: Ziff EB]]
-[[Category: double helix]]
-[[Category: protein-dna complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:43:41 2008''