+データを開く
-基本情報
登録情報 | データベース: SASBDB / ID: SASDA85 |
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試料 | CHD4 (PP-CC-AH-D)
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生物種 | Homo sapiens (ヒト) |
引用 | ジャーナル: J Mol Biol / 年: 2012 タイトル: The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. 著者: Aleksandra A Watson / Pravin Mahajan / Haydyn D T Mertens / Michael J Deery / Wenchao Zhang / Peter Pham / Xiuxia Du / Till Bartke / Wei Zhang / Christian Edlich / Georgina Berridge / Yun ...著者: Aleksandra A Watson / Pravin Mahajan / Haydyn D T Mertens / Michael J Deery / Wenchao Zhang / Peter Pham / Xiuxia Du / Till Bartke / Wei Zhang / Christian Edlich / Georgina Berridge / Yun Chen / Nicola A Burgess-Brown / Tony Kouzarides / Nicola Wiechens / Tom Owen-Hughes / Dmitri I Svergun / Opher Gileadi / Ernest D Laue / 要旨: The NuRD (nucleosome remodeling and deacetylase) complex serves as a crucial epigenetic regulator of cell differentiation, proliferation, and hematopoietic development by coupling the deacetylation ...The NuRD (nucleosome remodeling and deacetylase) complex serves as a crucial epigenetic regulator of cell differentiation, proliferation, and hematopoietic development by coupling the deacetylation and demethylation of histones, nucleosome mobilization, and the recruitment of transcription factors. The core nucleosome remodeling function of the mammalian NuRD complex is executed by the helicase-domain-containing ATPase CHD4 (Mi-2β) subunit, which also contains N-terminal plant homeodomain (PHD) and chromo domains. The mode of regulation of chromatin remodeling by CHD4 is not well understood, nor is the role of its PHD and chromo domains. Here, we use small-angle X-ray scattering, nucleosome binding ATPase and remodeling assays, limited proteolysis, cross-linking, and tandem mass spectrometry to propose a three-dimensional structural model describing the overall shape and domain interactions of CHD4 and discuss the relevance of these for regulating the remodeling of chromatin by the NuRD complex. |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-モデル
モデル #98 | タイプ: dummy / ソフトウェア: dammif / ダミー原子の半径: 3.60 A / カイ2乗値: 1.909924 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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モデル #102 | タイプ: dummy / ソフトウェア: monsa / ダミー原子の半径: 5.00 A / コメント: Combined multiphase model / カイ2乗値: 3.629025 Omokage検索でこの集合体の類似形状データを探す (詳細) |
モデル #103 | タイプ: dummy / ソフトウェア: monsa / ダミー原子の半径: 5.00 A / カイ2乗値: 3.629025 Omokage検索でこの集合体の類似形状データを探す (詳細) |
モデル #104 | タイプ: dummy / ソフトウェア: monsa / ダミー原子の半径: 5.00 A / カイ2乗値: 2.778889 |
モデル #105 | タイプ: dummy / ソフトウェア: monsa / ダミー原子の半径: 5.00 A / カイ2乗値: 1.098304 Omokage検索でこの集合体の類似形状データを探す (詳細) |
モデル #106 | タイプ: dummy / ソフトウェア: monsa / ダミー原子の半径: 5.00 A / カイ2乗値: 2.3716 |
-試料
試料 | 名称: CHD4 (PP-CC-AH-D) / Sample MW: 117.4 kDa / 試料濃度: 1.00-8.30 |
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バッファ | 名称: 50 mM HEPES / pH: 7.5 / 組成: 5.0% Glycerol, 300 mM NaCl |
要素 #81 | 名称: CHD4 (PP-CC-AH-D) / タイプ: protein / 記述: Human Chromatin Remodeler CHD4 (363-1353) / 分子量: 117.4 / 分子数: 1 / 由来: Homo sapiens 配列: MGHHHHHHSS GVDLGTENLY FQSMDGYETD HQDYCEVCQQ GGEIILCDTC PRAYHMVCLD PDMEKAPEGK WSCPHCEKEG IQWEAKEDNS EGEEILEEVG GDLEEEDDHH MEFCRVCKDG GELLCCDTCP SSYHIHCLNP PLPEIPNGEW LCPRCTCPAL KGKVQKILIW ...配列: MGHHHHHHSS GVDLGTENLY FQSMDGYETD HQDYCEVCQQ GGEIILCDTC PRAYHMVCLD PDMEKAPEGK WSCPHCEKEG IQWEAKEDNS EGEEILEEVG GDLEEEDDHH MEFCRVCKDG GELLCCDTCP SSYHIHCLNP PLPEIPNGEW LCPRCTCPAL KGKVQKILIW KWGQPPSPTP VPRPPDADPN TPSPKPLEGR PERQFFVKWQ GMSYWHCSWV SELQLELHCQ VMFRNYQRKN DMDEPPSGDF GGDEEKSRKR KNKDPKFAEM EERFYRYGIK PEWMMIHRIL NHSVDKKGHV HYLIKWRDLP YDQASWESED VEIQDYDLFK QSYWNHRELM RGEEGRPGKK LKKVKLRKLE RPPETPTVDP TVKYERQPEY LDATGGTLHP YQMEGLNWLR FSWAQGTDTI LADEMGLGKT VQTAVFLYSL YKEGHSKGPF LVSAPLSTII NWEREFEMWA PDMYVVTYVG DKDSRAIIRE NEFSFEDNAI RGGKKASRMK KEASVKFHVL LTSYELITID MAILGSIDWA CLIVDEAHRL KNNQSKFFRV LNGYSLQHKL LLTGTPLQNN LEELFHLLNF LTPERFHNLE GFLEEFADIA KEDQIKKLHD MLGPHMLRRL KADVFKNMPS KTELIVRVEL SPMQKKYYKY ILTRNFEALN ARGGGNQVSL LNVVMDLKKC CNHPYLFPVA AMEAPKMPNG MYDGSALIRA SGKLLLLQKM LKNLKEGGHR VLIFSQMTKM LDLLEDFLEH EGYKYERIDG GITGNMRQEA IDRFNAPGAQ QFCFLLSTRA GGLGINLATA DTVIIYDSDW NPHNDIQAFS RAHRIGQNKK VMIYRFVTRA SVEERITQVA KKKMMLTHLV VRPGLGSKTG SMSKQELDDI LKFGTEELFK DEATDGGGDN KEGEDSSVIH YDDKAIERLL DRNQDETEDT ELQGMNEYLS SFKVAQYVVR EEEMGEEEEV EREIIKQEES VDPDYWEKLL RHHYEQQQED LARNLGKGKR IRKQVNYNDG SQEDR |
-実験情報
ビーム | 設備名称: DORIS III X33 / 地域: Hamburg / 国: Germany / 形状: 0.6 / 線源: X-ray synchrotron / 波長: 0.15 Å / スペクトロメータ・検出器間距離: 2.7 mm | |||||||||||||||
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検出器 | 名称: Pilatus 1M-W / Pixsize x: 0.172 mm | |||||||||||||||
スキャン | タイトル: CHD4 (PP-CC-AH-D) / 測定日: 2010年11月13日 / 保管温度: 10 °C / セル温度: 10 °C / 照射時間: 15 sec. / フレーム数: 8 / 単位: 1/nm /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 4.5a / ポイント数: 436 /
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結果 | D max: 17.4 / カーブのタイプ: extrapolated / Standard: BSA コメント: The ATPase CHD4 mediates nucleosome remodeling by the NuRD (nucleosome remodeling and deacetylase) complex. The NuRD complex serves as a crucial epigenetic regulator of cell ...コメント: The ATPase CHD4 mediates nucleosome remodeling by the NuRD (nucleosome remodeling and deacetylase) complex. The NuRD complex serves as a crucial epigenetic regulator of cell differentiation, proliferation, and hematopoietic development by coupling the deacetylation and demethylation of histones, nucleosome mobilization, and the recruitment of transcription factors. The three dimensional small-angle X-ray scattering model of CHD4 helps to define its interdomain interactions, with cross linking and limited proteolysis studies used to validate the model. Functional and binding assays suggest a regulatory role for the PHD and chromo domains.
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