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基本情報
登録情報 | データベース: PDB / ID: 1m3v | ||||||
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タイトル | FLIN4: Fusion of the LIM binding domain of Ldb1 and the N-terminal LIM domain of LMO4 | ||||||
![]() | fusion of the LIM interacting domain of ldb1 and the N-terminal LIM domain of LMO4 | ||||||
![]() | METAL BINDING PROTEIN / LIM domain / fusion protein / LMO proteins / Ldb1 | ||||||
機能・相同性 | ![]() regulation of kinase activity / cellular component assembly / negative regulation of erythrocyte differentiation / cerebellar Purkinje cell differentiation / positive regulation of hemoglobin biosynthetic process / primitive erythrocyte differentiation / head development / beta-catenin-TCF complex / RUNX1 regulates transcription of genes involved in differentiation of HSCs / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery ...regulation of kinase activity / cellular component assembly / negative regulation of erythrocyte differentiation / cerebellar Purkinje cell differentiation / positive regulation of hemoglobin biosynthetic process / primitive erythrocyte differentiation / head development / beta-catenin-TCF complex / RUNX1 regulates transcription of genes involved in differentiation of HSCs / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / epithelial structure maintenance / LIM domain binding / gastrulation with mouth forming second / anterior/posterior axis specification / regulation of focal adhesion assembly / cell leading edge / somatic stem cell population maintenance / hair follicle development / positive regulation of cell adhesion / regulation of cell migration / cerebellum development / positive regulation of transcription elongation by RNA polymerase II / RNA polymerase II transcription regulator complex / Wnt signaling pathway / neuron differentiation / transcription regulator complex / DNA-binding transcription factor binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / transcription coactivator activity / cell adhesion / negative regulation of DNA-templated transcription / chromatin binding / chromatin / enzyme binding / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / nucleoplasm / identical protein binding / nucleus 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | 溶液NMR / simulated annealing, molecular dynamics torsion angle dynamics | ||||||
![]() | Deane, J.E. / Mackay, J.P. / Kwan, A.H.Y. / Sum, E.Y. / Visvader, J.E. / Matthews, J.M. | ||||||
![]() | ![]() タイトル: Structural basis for the recognition of ldb1 by the N-terminal LIM domains of LMO2 and LMO4 著者: Deane, J.E. / Mackay, J.P. / Kwan, A.H. / Sum, E.Y. / Visvader, J.E. / Matthews, J.M. #1: ![]() タイトル: 1H, 15N and 13C assignments of FLIN4, an intramolecular LMO4:ldb1 complex. 著者: Deane, J.E. / Visvader, J.E. / Mackay, J.P. / Matthews, J.M. #2: ![]() タイトル: Design, production and characterization of FLIN2 and FLIN4: the engineering of intramolecular ldb1:LMO complexes 著者: Deane, J.E. / Sum, E. / Mackay, J.P. / Lindeman, G.J. / Visvader, J.E. / Matthews, J.M. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 684.2 KB | 表示 | ![]() |
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PDB形式 | ![]() | 569.9 KB | 表示 | ![]() |
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その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 472.8 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 870.5 KB | 表示 | |
XML形式データ | ![]() | 100.7 KB | 表示 | |
CIF形式データ | ![]() | 96.9 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 1j2oC C: 同じ文献を引用 ( |
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リンク
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集合体
登録構造単位 | ![]()
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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: 13017.508 Da / 分子数: 1 / 変異: C37S, C49S / 由来タイプ: 組換発現 詳細: Fusion protein comprises LIM domain transcription factor LMO4 (residues 16-86) via glycine-rich linker (GGSGGHMGSGG), LIM domain-binding protein 1 (residues 300-339). 由来: (組換発現) ![]() ![]() ![]() ![]() |
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#2: 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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NMR実験の詳細 | Text: This structure was solved using triple resonance NMR techniques. In addition to the experiments listed above HNCO, HN(CA)CO, CC(CO)NH-TOCSY and HCC(CO)NH-TOCSY were also used for backbone and ...Text: This structure was solved using triple resonance NMR techniques. In addition to the experiments listed above HNCO, HN(CA)CO, CC(CO)NH-TOCSY and HCC(CO)NH-TOCSY were also used for backbone and side chain assignments. |
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試料調製
詳細 |
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試料状態 | pH: 7 / 圧: ambient / 温度: 298 K | ||||||||||||
結晶化 | *PLUS 手法: other / 詳細: NMR |
-NMR測定
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M |
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放射波長 | 相対比: 1 |
NMRスペクトロメーター | タイプ: Bruker DRX / 製造業者: Bruker / モデル: DRX / 磁場強度: 600 MHz |
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解析
NMR software |
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精密化 | 手法: simulated annealing, molecular dynamics torsion angle dynamics ソフトェア番号: 1 詳細: Structure calculations were performed using ARIA 1.1. Final structures are based on 1804 unambiguous and 81 ambiguous NOE-derived distance restraints and 112 angle constraints from coupling ...詳細: Structure calculations were performed using ARIA 1.1. Final structures are based on 1804 unambiguous and 81 ambiguous NOE-derived distance restraints and 112 angle constraints from coupling constant data and predictions from chemical shift analysis using TALOS. | ||||||||||||||||||||||||
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: 20 |