2ma5

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==Solution NMR structure of PHD type Zinc finger domain of Lysine-specific demethylase 5B (PLU-1/JARID1B) from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7375C==
==Solution NMR structure of PHD type Zinc finger domain of Lysine-specific demethylase 5B (PLU-1/JARID1B) from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7375C==
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<StructureSection load='2ma5' size='340' side='right' caption='[[2ma5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2ma5' size='340' side='right'caption='[[2ma5]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ma5]] 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=2MA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MA5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ma5]] 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=2MA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MA5 FirstGlance]. <br>
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</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>
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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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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">JARID1B, KDM5B, PLU1, RBBP2H1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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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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<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=2ma5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ma5 OCA], [http://pdbe.org/2ma5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ma5 RCSB], [http://www.ebi.ac.uk/pdbsum/2ma5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ma5 ProSAT]</span></td></tr>
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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=2ma5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ma5 OCA], [https://pdbe.org/2ma5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ma5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ma5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ma5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KDM5B_HUMAN KDM5B_HUMAN]] Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.<ref>PMID:12657635</ref> <ref>PMID:16645588</ref> <ref>PMID:17320161</ref> <ref>PMID:17363312</ref>
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[https://www.uniprot.org/uniprot/KDM5B_HUMAN KDM5B_HUMAN] Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.<ref>PMID:12657635</ref> <ref>PMID:16645588</ref> <ref>PMID:17320161</ref> <ref>PMID:17363312</ref>
==See Also==
==See Also==
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*[[Lysine-specific histone demethylase|Lysine-specific histone demethylase]]
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*[[Lysine-specific histone demethylase 3D structures|Lysine-specific histone demethylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Acton, T B]]
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[[Category: Large Structures]]
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[[Category: Cort, J R]]
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[[Category: Acton TB]]
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[[Category: Everett, J K]]
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[[Category: Cort JR]]
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[[Category: Hassan, F]]
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[[Category: Everett JK]]
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[[Category: Janjua, H]]
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[[Category: Hassan F]]
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[[Category: Kennedy, M A]]
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[[Category: Janjua H]]
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[[Category: Kohan, E]]
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[[Category: Kennedy MA]]
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[[Category: Lee, D]]
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[[Category: Kohan E]]
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[[Category: Montelione, G T]]
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[[Category: Lee D]]
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[[Category: Structural genomic]]
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[[Category: Montelione GT]]
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[[Category: Ramelot, T A]]
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[[Category: Ramelot TA]]
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[[Category: Xiao, R]]
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[[Category: Xiao R]]
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[[Category: Yang, Y]]
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[[Category: Yang Y]]
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[[Category: Nesg]]
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[[Category: Oxidoreductase]]
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[[Category: Phd]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Psi-biology]]
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[[Category: Zinc binding protein]]
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Current revision

Solution NMR structure of PHD type Zinc finger domain of Lysine-specific demethylase 5B (PLU-1/JARID1B) from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7375C

PDB ID 2ma5

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