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| | ==Crystal structure of ZMYND8 PHD-BROMO-PWWP tandem in complex with Drebrin ADF-H domain== | | ==Crystal structure of ZMYND8 PHD-BROMO-PWWP tandem in complex with Drebrin ADF-H domain== |
| - | <StructureSection load='5y1z' size='340' side='right' caption='[[5y1z]], [[Resolution|resolution]] 2.68Å' scene=''> | + | <StructureSection load='5y1z' size='340' side='right'caption='[[5y1z]], [[Resolution|resolution]] 2.68Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y1z]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y1Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y1z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y1Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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">X-ray diffraction, [[Resolution|Resolution]] 2.676Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DBN1, D0S117E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ZMYND8, KIAA1125, PRKCBP1, RACK7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5y1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1z OCA], [http://pdbe.org/5y1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y1z RCSB], [http://www.ebi.ac.uk/pdbsum/5y1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1z 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=5y1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1z OCA], [https://pdbe.org/5y1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y1z RCSB], [https://www.ebi.ac.uk/pdbsum/5y1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DREB_HUMAN DREB_HUMAN]] Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.<ref>PMID:20215400</ref> | + | [https://www.uniprot.org/uniprot/DREB_HUMAN DREB_HUMAN] Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.<ref>PMID:20215400</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Li, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Liu, H]] | + | [[Category: Li J]] |
| - | [[Category: Liu, W]] | + | [[Category: Liu H]] |
| - | [[Category: Wan, J]] | + | [[Category: Liu W]] |
| - | [[Category: Yao, N]] | + | [[Category: Wan J]] |
| - | [[Category: Zhang, M]] | + | [[Category: Yao N]] |
| - | [[Category: Actin binding]]
| + | [[Category: Zhang M]] |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
DREB_HUMAN Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS.[1]
Publication Abstract from PubMed
Malfunctions of the actin binding protein Drebrin have been implicated in various human diseases such as Alzheimer's disease, cognitive impairments, cancer, and digestive disorders, though with poorly understood mechanisms. The ADF-H domain of Drebrin does not contain actin binding and depolymerizing activity. Instead, it binds to a histone marker reader, ZMYND8. Here we present the high-resolution crystal structure of Drebrin ADF-H in complex with the ZMYND8 PHD-BROMO-PWWP tandem, elucidating the mechanistic basis governing the highly specific interaction of the two proteins. The structure reveals that the ZMYND8 PHD-BROMO-PWWP tandem forms a structural supramodule that is necessary for binding to Drebrin ADF-H. Drebrin ADF-H competes with modified histone for binding to ZMYND8. Binding of Drebrin can shuttle ZMYND8 from nucleus to cytoplasm in living cells. Taken together, our study uncovers a non-actin target binding mode for ADF-H domains, and suggests that Drebrin may regulate activities of epigenetic reader ZMYND8 via its cytoplasmic sequestration.
The Structure of the ZMYND8/Drebrin Complex Suggests a Cytoplasmic Sequestering Mechanism of ZMYND8 by Drebrin.,Yao N, Li J, Liu H, Wan J, Liu W, Zhang M Structure. 2017 Sep 13. pii: S0969-2126(17)30290-3. doi:, 10.1016/j.str.2017.08.014. PMID:28966017[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Perez-Martinez M, Gordon-Alonso M, Cabrero JR, Barrero-Villar M, Rey M, Mittelbrunn M, Lamana A, Morlino G, Calabia C, Yamazaki H, Shirao T, Vazquez J, Gonzalez-Amaro R, Veiga E, Sanchez-Madrid F. F-actin-binding protein drebrin regulates CXCR4 recruitment to the immune synapse. J Cell Sci. 2010 Apr 1;123(Pt 7):1160-70. doi: 10.1242/jcs.064238. Epub 2010 Mar , 9. PMID:20215400 doi:http://dx.doi.org/10.1242/jcs.064238
- ↑ Yao N, Li J, Liu H, Wan J, Liu W, Zhang M. The Structure of the ZMYND8/Drebrin Complex Suggests a Cytoplasmic Sequestering Mechanism of ZMYND8 by Drebrin. Structure. 2017 Sep 13. pii: S0969-2126(17)30290-3. doi:, 10.1016/j.str.2017.08.014. PMID:28966017 doi:http://dx.doi.org/10.1016/j.str.2017.08.014
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