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- SASDFV3: Cytokine-like nuclear factor dehydrogenase domain, NPAC DH (NPAC ... -
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Open data
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Basic information
Entry | ![]() |
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![]() | Cytokine-like nuclear factor dehydrogenase domain, NPAC DH (NPAC delta-261)
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Function / homology | ![]() chromatin-protein adaptor activity / transcription elongation-coupled chromatin remodeling / nucleosome binding / transcription initiation-coupled chromatin remodeling / methylated histone binding / NAD binding / nucleosome / NADP binding / histone binding / oxidoreductase activity ...chromatin-protein adaptor activity / transcription elongation-coupled chromatin remodeling / nucleosome binding / transcription initiation-coupled chromatin remodeling / methylated histone binding / NAD binding / nucleosome / NADP binding / histone binding / oxidoreductase activity / chromatin binding / chromatin / DNA binding / nucleoplasm / cytosol Similarity search - Function |
Biological species | ![]() |
![]() | ![]() Title: A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex. Authors: Chiara Marabelli / Biagina Marrocco / Simona Pilotto / Sagar Chittori / Sarah Picaud / Sara Marchese / Giuseppe Ciossani / Federico Forneris / Panagis Filippakopoulos / Guy Schoehn / Daniela ...Authors: Chiara Marabelli / Biagina Marrocco / Simona Pilotto / Sagar Chittori / Sarah Picaud / Sara Marchese / Giuseppe Ciossani / Federico Forneris / Panagis Filippakopoulos / Guy Schoehn / Daniela Rhodes / Sriram Subramaniam / Andrea Mattevi / ![]() ![]() ![]() ![]() ![]() ![]() Abstract: LSD1 and LSD2 are homologous histone demethylases with opposite biological outcomes related to chromatin silencing and transcription elongation, respectively. Unlike LSD1, LSD2 nucleosome-demethylase ...LSD1 and LSD2 are homologous histone demethylases with opposite biological outcomes related to chromatin silencing and transcription elongation, respectively. Unlike LSD1, LSD2 nucleosome-demethylase activity relies on a specific linker peptide from the multidomain protein NPAC. We used single-particle cryoelectron microscopy (cryo-EM), in combination with kinetic and mutational analysis, to analyze the mechanisms underlying the function of the human LSD2/NPAC-linker/nucleosome complex. Weak interactions between LSD2 and DNA enable multiple binding modes for the association of the demethylase to the nucleosome. The demethylase thereby captures mono- and dimethyl Lys4 of the H3 tail to afford histone demethylation. Our studies also establish that the dehydrogenase domain of NPAC serves as a catalytically inert oligomerization module. While LSD1/CoREST forms a nucleosome docking platform at silenced gene promoters, LSD2/NPAC is a multifunctional enzyme complex with flexible linkers, tailored for rapid chromatin modification, in conjunction with the advance of the RNA polymerase on actively transcribed genes. |
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Structure visualization
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | ![]() 4704C ![]() 4705C ![]() 4710C ![]() 4711C ![]() 4712C ![]() 6r1tC ![]() 6r1uC ![]() 6r25C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: Cytokine-like nuclear factor dehydrogenase domain, NPAC DH (NPAC delta-261) Specimen concentration: 1.5 mg/ml |
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Buffer | Name: 15 mM HEPES, 200 mM NaCl / pH: 7.3 |
Entity #1518 | Name: NPAC DH / Type: protein / Description: NPAC dehydrogenase domain / Formula weight: 31.369 / Num. of mol.: 4 / Source: Homo sapiens / References: UniProt: Q49A26 Sequence: GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA EKCDLFIQEG ARLGRTPAEV VSTCDITFAC VSDPKAAKDL VLGPSGVLQG IRPGKCYVDM STVDADTVTE LAQVIVSRGG RFLEAPVSGN QQLSNDGMLV ILAAGDRGLY EDCSSCFQAM GKTSFFLGEV ...Sequence: GSITPTDKKI GFLGLGLMGS GIVSNLLKMG HTVTVWNRTA EKCDLFIQEG ARLGRTPAEV VSTCDITFAC VSDPKAAKDL VLGPSGVLQG IRPGKCYVDM STVDADTVTE LAQVIVSRGG RFLEAPVSGN QQLSNDGMLV ILAAGDRGLY EDCSSCFQAM GKTSFFLGEV GNAAKMMLIV NMVQGSFMAT IAEGLTLAQV TGQSQQTLLD ILNQGQLASI FLDQKCQNIL QGNFKPDFYL KYIQKDLRLA IALGDAVNHP TPMAAAANEV YKRAKALDQS DNDMSAVYRA YIH |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Jan 26, 2018 / Storage temperature: 4 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 173 / Unit: 1/nm /
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Distance distribution function P(R) |
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Result |
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