- EMDB-6862: Cryo-EM Structure of human ATR-ATRIP complex -
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基本情報
登録情報
データベース: EMDB / ID: EMD-6862
タイトル
Cryo-EM Structure of human ATR-ATRIP complex
マップデータ
試料
複合体: ATR-ATRIP complex
タンパク質・ペプチド: Serine/threonine-protein kinase ATR
タンパク質・ペプチド: ATR-interacting protein
機能・相同性
機能・相同性情報
ATR-ATRIP complex / establishment of RNA localization to telomere / positive regulation of telomerase catalytic core complex assembly / MutSalpha complex binding / positive regulation of DNA damage response, signal transduction by p53 class mediator / establishment of protein-containing complex localization to telomere / response to xenobiotic stimulus => GO:0009410 / multicellular organism development / MutLalpha complex binding / regulation of double-strand break repair ...ATR-ATRIP complex / establishment of RNA localization to telomere / positive regulation of telomerase catalytic core complex assembly / MutSalpha complex binding / positive regulation of DNA damage response, signal transduction by p53 class mediator / establishment of protein-containing complex localization to telomere / response to xenobiotic stimulus => GO:0009410 / multicellular organism development / MutLalpha complex binding / regulation of double-strand break repair / nucleobase-containing compound metabolic process / K63-linked polyubiquitin modification-dependent protein binding / HDR through Single Strand Annealing (SSA) / protein localization to chromosome, telomeric region / Impaired BRCA2 binding to RAD51 / negative regulation of DNA replication / Presynaptic phase of homologous DNA pairing and strand exchange / replicative senescence / Regulation of HSF1-mediated heat shock response / Activation of ATR in response to replication stress / interstrand cross-link repair / regulation of cellular response to heat / positive regulation of telomere maintenance via telomerase / Meiotic synapsis / telomere maintenance / regulation of signal transduction by p53 class mediator / DNA damage checkpoint signaling / Fanconi Anemia Pathway / TP53 Regulates Transcription of DNA Repair Genes / G2/M DNA damage checkpoint / cellular response to gamma radiation / PML body / cellular response to UV / chromosome / Processing of DNA double-strand break ends / peptidyl-serine phosphorylation / DNA replication / Regulation of TP53 Activity through Phosphorylation / protein autophosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / DNA repair / protein serine/threonine kinase activity / DNA damage response / Golgi apparatus / DNA binding / nucleoplasm / ATP binding / nucleus 類似検索 - 分子機能
Strategic Priority Research Program of Chinese Academy of Sciences(CAS))
XDB08000000
中国
Ministry of Science and Technology (China)
2016YFA0501100
中国
National Natural Science Foundation of China
31425008
中国
National Natural Science Foundation of China
U1432242
中国
Beijing Municipal Science & Technology Commission
Z161100000116034
中国
National Natural Science Foundation of China
91419301
中国
引用
ジャーナル: Cell Res / 年: 2018 タイトル: Cryo-EM structure of human ATR-ATRIP complex. 著者: Qinhui Rao / Mengjie Liu / Yuan Tian / Zihan Wu / Yuhan Hao / Lei Song / Zhaoyu Qin / Chen Ding / Hong-Wei Wang / Jiawei Wang / Yanhui Xu / 要旨: ATR (ataxia telangiectasia-mutated and Rad3-related) protein kinase and ATRIP (ATR-interacting protein) form a complex and play a critical role in response to replication stress and DNA damage. Here, ...ATR (ataxia telangiectasia-mutated and Rad3-related) protein kinase and ATRIP (ATR-interacting protein) form a complex and play a critical role in response to replication stress and DNA damage. Here, we determined the cryo-electron microscopy (EM) structure of the human ATR-ATRIP complex at 4.7 Å resolution and built an atomic model of the C-terminal catalytic core of ATR (residues 1 521-2 644) at 3.9 Å resolution. The complex adopts a hollow "heart" shape, consisting of two ATR monomers in distinct conformations. The EM map for ATRIP reveals 14 HEAT repeats in an extended "S" shape. The conformational flexibility of ATR allows ATRIP to properly lock the N-termini of the two ATR monomers to favor ATR-ATRIP complex formation and functional diversity. The isolated "head-head" and "tail-tail" each adopts a pseudo 2-fold symmetry. The catalytic pockets face outward and substrate access is not restricted by inhibitory elements. Our studies provide a structural basis for understanding the assembly of the ATR-ATRIP complex and a framework for characterizing ATR-mediated DNA repair pathways.