+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2llq | ||||||
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タイトル | Solution nmr-derived structure of calmodulin c-lobe bound with er alpha peptide | ||||||
要素 |
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キーワード | METAL BINDING PROTEIN/HORMONE RECEPTOR / METAL BINDING PROTEIN-HORMONE RECEPTOR complex | ||||||
機能・相同性 | 機能・相同性情報 regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation / epithelial cell development / prostate epithelial cord elongation / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / TFIIB-class transcription factor binding / androgen metabolic process / steroid hormone receptor signaling pathway / mammary gland alveolus development / estrogen receptor signaling pathway / cellular response to estrogen stimulus / estrogen response element binding / : / enzyme regulator activity / nuclear receptor-mediated steroid hormone signaling pathway / negative regulation of canonical NF-kappaB signal transduction / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / protein localization to chromatin / 14-3-3 protein binding / TBP-class protein binding / nitric-oxide synthase regulator activity / steroid binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / ESR-mediated signaling / transcription corepressor binding / negative regulation of miRNA transcription / positive regulation of nitric-oxide synthase activity / cellular response to estradiol stimulus / transcription coregulator binding / stem cell differentiation / nuclear estrogen receptor binding / SUMOylation of intracellular receptors / euchromatin / negative regulation of DNA-binding transcription factor activity / beta-catenin binding / transcription coactivator binding / positive regulation of DNA-binding transcription factor activity / Nuclear Receptor transcription pathway / response to estrogen / Regulation of RUNX2 expression and activity / Constitutive Signaling by Aberrant PI3K in Cancer / nuclear receptor activity / male gonad development / positive regulation of nitric oxide biosynthetic process / sequence-specific double-stranded DNA binding / positive regulation of fibroblast proliferation / Ovarian tumor domain proteases / PIP3 activates AKT signaling / response to estradiol / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of cytosolic calcium ion concentration / ATPase binding / regulation of inflammatory response / fibroblast proliferation / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / DNA-binding transcription activator activity, RNA polymerase II-specific / Estrogen-dependent gene expression / transcription regulator complex / Extra-nuclear estrogen signaling / calmodulin binding / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of gene expression / signaling receptor binding / calcium ion binding / chromatin binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / protein kinase binding / positive regulation of DNA-templated transcription / Golgi apparatus / enzyme binding / negative regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / identical protein binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | Xenopus laevis (アフリカツメガエル) Homo sapiens (ヒト) | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
データ登録者 | Zhang, Y. | ||||||
引用 | ジャーナル: J.Biol.Chem. / 年: 2012 タイトル: Structural basis for Ca2+-induced activation and dimerization of estrogen receptor alpha by calmodulin. 著者: Zhang, Y. / Li, Z. / Sacks, D.B. / Ames, J.B. | ||||||
履歴 |
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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
-ダウンロード
PDBx/mmCIF形式 | 2llq.cif.gz | 300.5 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2llq.ent.gz | 251.5 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2llq.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 2llq_validation.pdf.gz | 414.4 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 2llq_full_validation.pdf.gz | 520.5 KB | 表示 | |
XML形式データ | 2llq_validation.xml.gz | 17.6 KB | 表示 | |
CIF形式データ | 2llq_validation.cif.gz | 28.5 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ll/2llq ftp://data.pdbj.org/pub/pdb/validation_reports/ll/2llq | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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NMR アンサンブル |
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-要素
#1: タンパク質 | 分子量: 7737.468 Da / 分子数: 1 / 断片: EF-hand domains 3 and 4, residues 83-149 / 由来タイプ: 組換発現 由来: (組換発現) Xenopus laevis (アフリカツメガエル) 遺伝子: calm1, calm2 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P62155, UniProt: P0DP33*PLUS |
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#2: タンパク質・ペプチド | 分子量: 2202.645 Da / 分子数: 1 / 断片: UNP residues 287-305 / 由来タイプ: 合成 / 由来: (合成) Homo sapiens (ヒト) / 参照: UniProt: P03372 |
#3: 化合物 |
-実験情報
-実験
実験 | 手法: 溶液NMR | ||||||||||||||||
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NMR実験 |
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-試料調製
詳細 | 内容: 1 mM [U-100% 13C; U-100% 15N] protein, 93% H2O/7% D2O 溶媒系: 93% H2O/7% D2O |
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試料 | 濃度: 1 mM / 構成要素: entity_1-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] |
試料状態 | イオン強度: 0.02 / pH: 7.0 / 圧: ambient / 温度: 310 K |
-NMR測定
NMRスペクトロメーター | タイプ: Bruker Avance / 製造業者: Bruker / モデル: AVANCE / 磁場強度: 800 MHz |
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-解析
NMR software |
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精密化 | 手法: simulated annealing / ソフトェア番号: 1 | ||||||||||||
代表構造 | 選択基準: lowest energy | ||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 200 / 登録したコンフォーマーの数: 10 |