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1mm3

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Current revision

Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF

Structural highlights

1mm3 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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

↑ Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL. Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature. 1998 Oct 29;395(6705):917-21. PMID:9804427 doi:http://dx.doi.org/10.1038/27699
↑ Sillibourne JE, Delaval B, Redick S, Sinha M, Doxsey SJ. Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity. Mol Biol Cell. 2007 Sep;18(9):3667-80. Epub 2007 Jul 11. PMID:17626165 doi:http://dx.doi.org/10.1091/mbc.E06-07-0604
↑ Kwan AH, Gell DA, Verger A, Crossley M, Matthews JM, Mackay JP. Engineering a protein scaffold from a PHD finger. Structure. 2003 Jul;11(7):803-13. PMID:12842043

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mm3"

@@ Line 1: / Line 1: @@
 ==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]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mm3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MM3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mm3]] 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=1MM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MM3 FirstGlance]. <br>
-</td></tr><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mm2|1mm2]], [[1fp0|1fp0]], [[1f62|1f62]]</div></td></tr>
+<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>
-<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'>[https://proteopedia.org/fgij/fg.htm?mol=1mm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm3 OCA], [https://pdbe.org/1mm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mm3 RCSB], [https://www.ebi.ac.uk/pdbsum/1mm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mm3 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 == Function ==
-[[http://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>
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Crossley, M]]
+[[Category: Crossley M]]
-[[Category: Gell, D A]]
+[[Category: Gell DA]]
-[[Category: Kwan, A H.Y]]
+[[Category: Kwan AHY]]
-[[Category: Mackay, J P]]
+[[Category: Mackay JP]]
-[[Category: Matthews, J M]]
+[[Category: Matthews JM]]
-[[Category: Verger, A]]
+[[Category: Verger A]]
-[[Category: Dna binding protein-transcription complex]]
-[[Category: Phd]]
-[[Category: Protein scaffold]]
-[[Category: Zinc finger]]

1mm3

From Proteopedia

Current revision

Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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