1mm3: Difference between revisions
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==Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF== | ==Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF== | ||
<StructureSection load='1mm3' size='340' side='right' caption='[[1mm3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1mm3' size='340' side='right' caption='[[1mm3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mm2|1mm2]], [[1fp0|1fp0]], [[1f62|1f62]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mm2|1mm2]], [[1fp0|1fp0]], [[1f62|1f62]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHD4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHD4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1mm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm3 OCA], [http://pdbe.org/1mm3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mm3 RCSB], [http://www.ebi.ac.uk/pdbsum/1mm3 PDBsum]</span></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=1mm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm3 OCA], [http://pdbe.org/1mm3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mm3 RCSB], [http://www.ebi.ac.uk/pdbsum/1mm3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mm3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=1mm3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1mm3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1mm3" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:09, 25 October 2017
Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTFSolution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF
Structural highlights
Function[CHD4_HUMAN] Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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