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データを開く
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基本情報
| 登録情報 | データベース: PDB / ID: 5ijn | ||||||
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| タイトル | Composite structure of the inner ring of the human nuclear pore complex (32 copies of Nup205) | ||||||
要素 |
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キーワード | TRANSPORT PROTEIN / Nuclear pore complex / Nucleocytoplasmic transport | ||||||
| 機能・相同性 | 機能・相同性情報centriole assembly / positive regulation of centriole replication / regulation of protein import into nucleus / regulation of Ras protein signal transduction / positive regulation of mitotic cytokinetic process / protein localization to nuclear inner membrane / nuclear envelope organization / nuclear pore inner ring / nuclear pore central transport channel / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery ...centriole assembly / positive regulation of centriole replication / regulation of protein import into nucleus / regulation of Ras protein signal transduction / positive regulation of mitotic cytokinetic process / protein localization to nuclear inner membrane / nuclear envelope organization / nuclear pore inner ring / nuclear pore central transport channel / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore complex assembly / nuclear pore organization / atrial cardiac muscle cell action potential / positive regulation of protein localization to centrosome / Nuclear Pore Complex (NPC) Disassembly / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Transport of Ribonucleoproteins into the Host Nucleus / miRNA processing / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / negative regulation of Ras protein signal transduction / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / NLS-bearing protein import into nucleus / structural constituent of nuclear pore / Transport of Mature mRNA Derived from an Intronless Transcript / nuclear localization sequence binding / Flemming body / Rev-mediated nuclear export of HIV RNA / SUMOylation of RNA binding proteins / Nuclear import of Rev protein / mitotic centrosome separation / Transport of Mature mRNA derived from an Intron-Containing Transcript / NEP/NS2 Interacts with the Cellular Export Machinery / RNA export from nucleus / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / centrosome cycle / negative regulation of programmed cell death / nucleocytoplasmic transport / positive regulation of epidermal growth factor receptor signaling pathway / Viral Messenger RNA Synthesis / PTB domain binding / poly(A)+ mRNA export from nucleus / mitotic metaphase chromosome alignment / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / negative regulation of epidermal growth factor receptor signaling pathway / SUMOylation of DNA replication proteins / positive regulation of SMAD protein signal transduction / Regulation of HSF1-mediated heat shock response / regulation of signal transduction / mRNA transport / nuclear pore / mRNA export from nucleus / SUMOylation of DNA damage response and repair proteins / positive regulation of mitotic nuclear division / Hsp70 protein binding / nuclear periphery / SH2 domain binding / regulation of mitotic spindle organization / SUMOylation of chromatin organization proteins / ubiquitin binding / HCMV Late Events / Hsp90 protein binding / Transcriptional regulation by small RNAs / phospholipid binding / ISG15 antiviral mechanism / protein import into nucleus / HCMV Early Events / spindle pole / mitotic spindle / cellular senescence / nuclear envelope / protein transport / signaling receptor complex adaptor activity / snRNP Assembly / nuclear membrane / cell surface receptor signaling pathway / positive regulation of canonical NF-kappaB signal transduction / ribonucleoprotein complex / negative regulation of cell population proliferation / chromatin binding / centrosome / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / protein-containing complex binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / nucleoplasm / identical protein binding / membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
| 生物種 | Homo sapiens (ヒト) | ||||||
| 手法 | 電子顕微鏡法 / サブトモグラム平均法 / クライオ電子顕微鏡法 / 解像度: 21.4 Å | ||||||
データ登録者 | Kosinski, J. / Mosalaganti, S. / von Appen, A. / Beck, M. | ||||||
| 資金援助 | ドイツ, 1件
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引用 | ジャーナル: Science / 年: 2016タイトル: Molecular architecture of the inner ring scaffold of the human nuclear pore complex. 著者: Jan Kosinski / Shyamal Mosalaganti / Alexander von Appen / Roman Teimer / Amanda L DiGuilio / William Wan / Khanh Huy Bui / Wim J H Hagen / John A G Briggs / Joseph S Glavy / Ed Hurt / Martin Beck / ![]() 要旨: Nuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these ...Nuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these nucleoporins assemble into the NPC scaffold imposes a formidable challenge. Recently, it has been shown how the Y complex, a prominent NPC module, forms the outer rings of the nuclear pore. However, the organization of the inner ring has remained unknown until now. We used molecular modeling combined with cross-linking mass spectrometry and cryo-electron tomography to obtain a composite structure of the inner ring. This architectural map explains the vast majority of the electron density of the scaffold. We conclude that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar. | ||||||
| 履歴 |
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構造の表示
| ムービー |
ムービービューア |
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| 構造ビューア | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 5ijn.cif.gz | 15.5 MB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb5ijn.ent.gz | 10.4 MB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 5ijn.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 | 5ijn_validation.pdf.gz | 2.6 MB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 5ijn_full_validation.pdf.gz | 6.9 MB | 表示 | |
| XML形式データ | 5ijn_validation.xml.gz | 2.2 MB | 表示 | |
| CIF形式データ | 5ijn_validation.cif.gz | 3.4 MB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ij/5ijn ftp://data.pdbj.org/pub/pdb/validation_reports/ij/5ijn | HTTPS FTP |
-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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| 1 | x 8![]()
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| モデル数 | 8 |
| 対称性 | 点対称性: (シェーンフリース記号: C8 (8回回転対称)) |
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要素
-NUCLEAR PORE COMPLEX PROTEIN ... , 5種, 22分子 ABEKQWCIOUDJPVFLRXGMSY
| #1: タンパク質 | 分子量: 155357.281 Da / 分子数: 6 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 細胞株: HELA / 細胞株 (発現宿主): HELA / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: O75694#2: タンパク質 | 分子量: 93599.102 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 細胞株: HELA / 細胞株 (発現宿主): HELA / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q8N1F7#3: タンパク質 | 分子量: 228172.875 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 細胞株: HELA / 細胞株 (発現宿主): HELA / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q92621#4: タンパク質 | 分子量: 55491.156 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 細胞株: HELA / 細胞株 (発現宿主): HELA / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q7Z3B4#5: タンパク質 | 分子量: 60941.480 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 細胞株: HELA / 細胞株 (発現宿主): HELA / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q9BVL2 |
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-タンパク質 , 1種, 4分子 HNTZ
| #6: タンパク質 | 分子量: 53289.574 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 細胞株: HELA / 遺伝子: NUP62 / 細胞株 (発現宿主): HELA / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P37198 |
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-実験情報
-実験
| 実験 | 手法: 電子顕微鏡法 |
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| EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: サブトモグラム平均法 |
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試料調製
| 構成要素 | 名称: Nuclear envelope / タイプ: COMPLEX / Entity ID: #1-#7 / 由来: MULTIPLE SOURCES |
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| 分子量 | 値: 23 MDa / 実験値: NO |
| 緩衝液 | pH: 7.5 |
| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
| 急速凍結 | 凍結剤: ETHANE-PROPANE |
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電子顕微鏡撮影
| 実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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| 顕微鏡 | モデル: FEI TITAN KRIOS |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: OTHER |
| 電子レンズ | モード: BRIGHT FIELD |
| 撮影 | 電子線照射量: 3 e/Å2 / 検出モード: SUPER-RESOLUTION フィルム・検出器のモデル: GATAN K2 QUANTUM (4k x 4k) |
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解析
| EMソフトウェア |
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| EM 3D crystal entity | ∠α: 90 ° / ∠β: 90 ° / ∠γ: 90 ° / A: 1 Å / B: 1 Å / C: 1 Å / 空間群名: P1 / 空間群番号: 1 | ||||||||||||||||
| CTF補正 | タイプ: PHASE FLIPPING ONLY | ||||||||||||||||
| 対称性 | 点対称性: C1 (非対称) | ||||||||||||||||
| 3次元再構成 | 解像度: 21.4 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 8400 / 対称性のタイプ: POINT | ||||||||||||||||
| EM volume selection | Num. of tomograms: 101 / Num. of volumes extracted: 1112 | ||||||||||||||||
| 原子モデル構築 | プロトコル: RIGID BODY FIT 詳細: this pdb structure includes unambiguous fits only, .i.e. excluding the middle domain of nup205. the structure with that domain can be obtained from authors. protein-protein interfaces shall ...詳細: this pdb structure includes unambiguous fits only, .i.e. excluding the middle domain of nup205. the structure with that domain can be obtained from authors. protein-protein interfaces shall not be interpreted at residue-level resolution. this pdb structure contains eight models. the model 1 corresponds to the composite structure reported in the journal article associated with this entry. models 2-8 corresponds to the seven best scoring models automatically generated as described in the article. |
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万見について




Homo sapiens (ヒト)
ドイツ, 1件
引用

UCSF Chimera




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