1mm2

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[[Image:1mm2.gif|left|200px]]
 
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{{Structure
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==Solution structure of the 2nd PHD domain from Mi2b==
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|PDB= 1mm2 |SIZE=350|CAPTION= <scene name='initialview01'>1mm2</scene>
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<StructureSection load='1mm2' size='340' side='right'caption='[[1mm2]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1mm2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MM2 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= CHD4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=1mm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm2 OCA], [https://pdbe.org/1mm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mm2 RCSB], [https://www.ebi.ac.uk/pdbsum/1mm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mm2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHD4_HUMAN CHD4_HUMAN] Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.<ref>PMID:9804427</ref> <ref>PMID:17626165</ref>
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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/mm/1mm2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1mm2 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 design of proteins with tailored functions remains a relatively elusive goal. Small size, a well-defined structure, and the ability to maintain structural integrity despite multiple mutations are all desirable properties for such designer proteins. Many zinc binding domains fit this description. We determined the structure of a PHD finger from the transcriptional cofactor Mi2beta and investigated the suitability of this domain as a scaffold for presenting selected binding functions. The two flexible loops in the structure were mutated extensively by either substitution or expansion, without affecting the overall fold of the domain. A binding site for the corepressor CtBP2 was also grafted onto the domain, creating a new PHD domain that can specifically bind CtBP2 both in vitro and in the context of a eukaryotic cell nucleus. These results represent a step toward designing new regulatory proteins for modulating aberrant gene expression in vivo.
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'''Solution structure of the 2nd PHD domain from Mi2b'''
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Engineering a protein scaffold from a PHD finger.,Kwan AH, Gell DA, Verger A, Crossley M, Matthews JM, Mackay JP Structure. 2003 Jul;11(7):803-13. PMID:12842043<ref>PMID:12842043</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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<div class="pdbe-citations 1mm2" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The design of proteins with tailored functions remains a relatively elusive goal. Small size, a well-defined structure, and the ability to maintain structural integrity despite multiple mutations are all desirable properties for such designer proteins. Many zinc binding domains fit this description. We determined the structure of a PHD finger from the transcriptional cofactor Mi2beta and investigated the suitability of this domain as a scaffold for presenting selected binding functions. The two flexible loops in the structure were mutated extensively by either substitution or expansion, without affecting the overall fold of the domain. A binding site for the corepressor CtBP2 was also grafted onto the domain, creating a new PHD domain that can specifically bind CtBP2 both in vitro and in the context of a eukaryotic cell nucleus. These results represent a step toward designing new regulatory proteins for modulating aberrant gene expression in vivo.
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*[[Chromodomain-helicase-DNA-binding protein 3D structures|Chromodomain-helicase-DNA-binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1MM2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM2 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Engineering a protein scaffold from a PHD finger., Kwan AH, Gell DA, Verger A, Crossley M, Matthews JM, Mackay JP, Structure. 2003 Jul;11(7):803-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12842043 12842043]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Crossley, M.]]
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[[Category: Crossley M]]
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[[Category: Gell, D A.]]
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[[Category: Gell DA]]
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[[Category: Kwan, A H.Y.]]
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[[Category: Kwan AHY]]
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[[Category: Mackay, J P.]]
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[[Category: Mackay JP]]
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[[Category: Matthews, J M.]]
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[[Category: Matthews JM]]
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[[Category: Verger, A.]]
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[[Category: Verger A]]
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[[Category: ZN]]
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[[Category: phd]]
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[[Category: protein scaffold]]
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[[Category: zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:08 2008''
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Current revision

Solution structure of the 2nd PHD domain from Mi2b

PDB ID 1mm2

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OCA

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