|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of BRD1 PHD2 finger== | | ==Solution structure of BRD1 PHD2 finger== |
| - | <StructureSection load='2lq6' size='340' side='right' caption='[[2lq6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lq6' size='340' side='right'caption='[[2lq6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lq6]] 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=2LQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LQ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQ6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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">BRD1, BRL, BRPF2 ([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">BRD1, BRL, BRPF2 ([https://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=2lq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq6 OCA], [http://pdbe.org/2lq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lq6 RCSB], [http://www.ebi.ac.uk/pdbsum/2lq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lq6 ProSAT]</span></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=2lq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq6 OCA], [https://pdbe.org/2lq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lq6 RCSB], [https://www.ebi.ac.uk/pdbsum/2lq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lq6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BRD1_HUMAN BRD1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.<ref>PMID:16387653</ref> <ref>PMID:21880731</ref> | + | [[https://www.uniprot.org/uniprot/BRD1_HUMAN BRD1_HUMAN]] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.<ref>PMID:16387653</ref> <ref>PMID:21880731</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 21: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Bromodomain-containing protein|Bromodomain-containing protein]] | + | *[[Bromodomain-containing protein 3D structures|Bromodomain-containing protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 27: |
Line 27: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Liu, L]] | | [[Category: Liu, L]] |
| | [[Category: Wu, J]] | | [[Category: Wu, J]] |
| | [[Category: Metal binding protein]] | | [[Category: Metal binding protein]] |
| | [[Category: Phd finger]] | | [[Category: Phd finger]] |
| Structural highlights
Function
[BRD1_HUMAN] Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.[1] [2]
Publication Abstract from PubMed
Plant homeodomain (PHD) finger is found to be a versatile reader that functions in recruiting transcription factors and chromatin modification complexes. Bromodomain- and PHD finger-containing (BRPF) proteins are identified as scaffold component in a couple of histone acetyltransferase (HATs) complexes but the biological function of PHD fingers, composing the motif called PZPM (PHD/Zn-knuckle/PHD Motif), in BRPF proteins is far from being well understood. Here we report the three-dimensional solution structure of the second PHD finger of PZPM in human BRPF2. According to the structure, BRPF2 PHD2 possesses a two-strand beta sheet which is different from any other PHD fingers. Functionally, this PHD finger can potentially bind DNA non-specifically with an evolutionarily conserved and positively charged surface. We provide the structural and interaction information of this atypical PHD finger and categorize this BRPF2 PHD2 into a new subset of PHD finger. Moreover our work also shed light on the functional aspect of the PZPM.
Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA.,Liu L, Qin S, Zhang J, Ji P, Shi Y, Wu J J Struct Biol. 2012 Oct;180(1):165-73. doi: 10.1016/j.jsb.2012.06.014. Epub 2012 , Jul 20. PMID:22820306[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell. 2006 Jan 6;21(1):51-64. PMID:16387653 doi:10.1016/j.molcel.2005.12.007
- ↑ Qin S, Jin L, Zhang J, Liu L, Ji P, Wu M, Wu J, Shi Y. Recognition of unmodified histone H3 by the first PHD finger of bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and MOZ-related factor (MORF). J Biol Chem. 2011 Oct 21;286(42):36944-55. doi: 10.1074/jbc.M111.244400. Epub, 2011 Aug 31. PMID:21880731 doi:http://dx.doi.org/10.1074/jbc.M111.244400
- ↑ Liu L, Qin S, Zhang J, Ji P, Shi Y, Wu J. Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA. J Struct Biol. 2012 Oct;180(1):165-73. doi: 10.1016/j.jsb.2012.06.014. Epub 2012 , Jul 20. PMID:22820306 doi:http://dx.doi.org/10.1016/j.jsb.2012.06.014
|
