登録情報 | データベース: PDB / ID: 6jpv |
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タイトル | Structural analysis of AIMP2-DX2 and HSP70 interaction |
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要素 | Heat shock 70 kDa protein 1A,Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 |
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キーワード | CHAPERONE / HSP70 / AIMP2-DX2 / substrate binding domain |
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機能・相同性 | 機能・相同性情報
type II pneumocyte differentiation / : / Selenoamino acid metabolism / denatured protein binding / cellular heat acclimation / negative regulation of inclusion body assembly / death receptor agonist activity / Viral RNP Complexes in the Host Cell Nucleus / C3HC4-type RING finger domain binding / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway ...type II pneumocyte differentiation / : / Selenoamino acid metabolism / denatured protein binding / cellular heat acclimation / negative regulation of inclusion body assembly / death receptor agonist activity / Viral RNP Complexes in the Host Cell Nucleus / C3HC4-type RING finger domain binding / positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / Cytosolic tRNA aminoacylation / aminoacyl-tRNA synthetase multienzyme complex / ATP-dependent protein disaggregase activity / positive regulation of microtubule nucleation / misfolded protein binding / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / positive regulation of tumor necrosis factor-mediated signaling pathway / regulation of mitotic spindle assembly / aggresome / lysosomal transport / cellular response to steroid hormone stimulus / mRNA catabolic process / : / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / regulation of protein ubiquitination / Regulation of HSF1-mediated heat shock response / HSF1-dependent transactivation / response to unfolded protein / cellular response to unfolded protein / Mitochondrial unfolded protein response (UPRmt) / Attenuation phase / chaperone-mediated protein complex assembly / transcription regulator inhibitor activity / ATP metabolic process / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / inclusion body / heat shock protein binding / negative regulation of protein ubiquitination / centriole / Transcriptional and post-translational regulation of MITF-M expression and activity / protein folding chaperone / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / positive regulation of erythrocyte differentiation / positive regulation of RNA splicing / positive regulation of protein ubiquitination / positive regulation of interleukin-8 production / AUF1 (hnRNP D0) binds and destabilizes mRNA / negative regulation of transforming growth factor beta receptor signaling pathway / ATP-dependent protein folding chaperone / G protein-coupled receptor binding / negative regulation of cell growth / PKR-mediated signaling / histone deacetylase binding / positive regulation of NF-kappaB transcription factor activity / transcription corepressor activity / disordered domain specific binding / unfolded protein binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / cellular response to heat / virus receptor activity / protein refolding / cellular response to oxidative stress / protein-containing complex assembly / molecular adaptor activity / vesicle / blood microparticle / ficolin-1-rich granule lumen / protein stabilization / nuclear speck / protein ubiquitination / cadherin binding / receptor ligand activity / translation / ribonucleoprotein complex / signaling receptor binding / negative regulation of cell population proliferation / focal adhesion / apoptotic process / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / positive regulation of gene expression / negative regulation of apoptotic process / perinuclear region of cytoplasm / enzyme binding / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / protein-containing complex / ATP hydrolysis activity / mitochondrion / extracellular space / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / membrane / plasma membrane / cytosol類似検索 - 分子機能 AIMP2, lysyl-tRNA synthetase binding domain / AIMP2, thioredoxin-like domain / Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 / AIMP2 lysyl-tRNA synthetase binding domain / Thioredoxin-like domain / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. ...AIMP2, lysyl-tRNA synthetase binding domain / AIMP2, thioredoxin-like domain / Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 / AIMP2 lysyl-tRNA synthetase binding domain / Thioredoxin-like domain / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Substrate Binding Domain Of DNAk; Chain A, domain 1 / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Glutathione S-transferase, C-terminal domain / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Heat shock protein 70kD, C-terminal domain superfamily / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal domain superfamily / ATPase, nucleotide binding domain / Sandwich / Mainly Beta類似検索 - ドメイン・相同性 Heat shock 70 kDa protein 1A / Aminoacyl tRNA synthase complex-interacting multifunctional protein 2類似検索 - 構成要素 |
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生物種 | Homo sapiens (ヒト) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.15000649024 Å |
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データ登録者 | Cho, H.Y. / Son, S.Y. / Jeon, Y.H. |
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資金援助 | 韓国, 1件 組織 | 認可番号 | 国 |
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National Research Foundation (Korea) | NRF-2013M3A6A4045160 | 韓国 |
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引用 | ジャーナル: Nat.Chem.Biol. / 年: 2020 タイトル: Targeting the interaction of AIMP2-DX2 with HSP70 suppresses cancer development. 著者: Lim, S. / Cho, H.Y. / Kim, D.G. / Roh, Y. / Son, S.Y. / Mushtaq, A.U. / Kim, M. / Bhattarai, D. / Sivaraman, A. / Lee, Y. / Lee, J. / Yang, W.S. / Kim, H.K. / Kim, M.H. / Lee, K. / Jeon, Y.H. / Kim, S. |
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履歴 | 登録 | 2019年3月28日 | 登録サイト: PDBJ / 処理サイト: PDBJ |
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改定 1.0 | 2019年10月2日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2019年11月20日 | Group: Database references / カテゴリ: citation / Item: _citation.pdbx_database_id_DOI / _citation.title |
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改定 1.2 | 2019年12月18日 | Group: Database references / カテゴリ: citation / citation_author / Item: _citation.pdbx_database_id_PubMed |
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改定 1.3 | 2020年1月1日 | Group: Database references / カテゴリ: citation / citation_author Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year / _citation_author.identifier_ORCID |
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改定 1.4 | 2023年11月22日 | Group: Data collection / Database references / Refinement description カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id |
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