+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2oii | ||||||
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タイトル | Structure of EMILIN-1 C1q-like domain | ||||||
要素 | EMILIN-1 | ||||||
キーワード | STRUCTURAL PROTEIN / Emilin-1 / C1q-like domain / homotrimeric protein complex / beta-sandwich | ||||||
機能・相同性 | 機能・相同性情報 EMILIN complex / negative regulation of collagen fibril organization / extracellular matrix constituent conferring elasticity / negative regulation of macrophage migration / negative regulation of cell activation / integrin alpha4-beta1 complex / integrin binding involved in cell-matrix adhesion / elastic fiber assembly / positive regulation of defense response to bacterium / negative regulation of vascular endothelial growth factor signaling pathway ...EMILIN complex / negative regulation of collagen fibril organization / extracellular matrix constituent conferring elasticity / negative regulation of macrophage migration / negative regulation of cell activation / integrin alpha4-beta1 complex / integrin binding involved in cell-matrix adhesion / elastic fiber assembly / positive regulation of defense response to bacterium / negative regulation of vascular endothelial growth factor signaling pathway / negative regulation of collagen biosynthetic process / positive regulation of extracellular matrix assembly / collagen trimer / positive regulation of platelet aggregation / aortic valve morphogenesis / positive regulation of cell-substrate adhesion / Molecules associated with elastic fibres / cell adhesion mediated by integrin / negative regulation of vascular endothelial growth factor receptor signaling pathway / negative regulation of SMAD protein signal transduction / positive regulation of blood coagulation / cell-matrix adhesion / negative regulation of angiogenesis / negative regulation of cell migration / negative regulation of transforming growth factor beta receptor signaling pathway / negative regulation of ERK1 and ERK2 cascade / regulation of blood pressure / positive regulation of angiogenesis / cell migration / regulation of cell population proliferation / collagen-containing extracellular matrix / molecular adaptor activity / cell adhesion / positive regulation of apoptotic process / negative regulation of gene expression / positive regulation of gene expression / extracellular space / extracellular exosome / extracellular region / identical protein binding 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
データ登録者 | Verdone, G. / Colebrooke, S.A. / Corazza, A. / Cicero, D.O. / Eliseo, T. / Viglino, P. / Campbell, I.D. / Colombatti, A. / Esposito, G. | ||||||
引用 | ジャーナル: To be Published タイトル: The solution structure of the C-terminal domain of EMILIN-1 著者: Verdone, G. / Colebrooke, S.A. / Corazza, A. / Cicero, D.O. / Eliseo, T. / Viglino, P. / Campbell, I.D. / Colombatti, A. / Esposito, G. #1: ジャーナル: J.Biomol.NMR / 年: 2004 タイトル: Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1 著者: Verdone, G. / Colebrooke, S.A. / Boyd, J. / Viglino, P. / Corazza, A. / Doliana, R. / Mungiguerra, G. / Colombatti, A. / Esposito, G. / Campbell, I.D. #2: ジャーナル: J.Biol.Chem. / 年: 2000 タイトル: Self-assembly and supramolecular organization of Emillin 著者: Mongiat, M. / Mungiguerra, G. / Bot, S. / Mucignat, M.T. / Giacomello, E. / Doliana, R. / Colombatti, A. | ||||||
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 | 2oii.cif.gz | 1.2 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2oii.ent.gz | 995.3 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2oii.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 | 2oii_validation.pdf.gz | 381.7 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 2oii_full_validation.pdf.gz | 640.6 KB | 表示 | |
XML形式データ | 2oii_validation.xml.gz | 93.5 KB | 表示 | |
CIF形式データ | 2oii_validation.cif.gz | 118.5 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/oi/2oii ftp://data.pdbj.org/pub/pdb/validation_reports/oi/2oii | 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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NMR アンサンブル |
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-要素
#1: タンパク質 | 分子量: 17227.217 Da / 分子数: 3 / 断片: C-Terminal domain, C1q domain / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EMILIN1, EMI / 細胞株 (発現宿主): M15 cells / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: Q9Y6C2 |
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-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 |
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試料状態 | イオン強度: 20 mM Phosphate buffer, 100 mM NaCl / pH: 7.5 / 圧: 1 atm / 温度: 310 K |
-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 |
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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 詳細: The structure was obtained as the refinement of the homology model of emilin trimer C1q-domain based on the chain A of ACRP-30 crystal structure. The quaternary structure of C1q-domain ...詳細: The structure was obtained as the refinement of the homology model of emilin trimer C1q-domain based on the chain A of ACRP-30 crystal structure. The quaternary structure of C1q-domain homology model was built with a three-fold simmetry axis. The region between Tyr927 and Gly945 was not modelled and was not included in the refinement. Dihedral angles (obtained with TALOS), RDC values, NOE constraints were used in the refinement procedure. | ||||||||||||||||||||||||
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: 100 / 登録したコンフォーマーの数: 10 |