登録情報 | データベース: PDB / ID: 6n8y |
---|
タイトル | Hsp90-beta bound to PU-11-trans |
---|
要素 | Heat shock protein HSP 90-beta |
---|
キーワード | chaperone/chaperone inhibitor / HSP90 / Inhibitor / Cancer / Cytosol / CHAPERONE / chaperone-chaperone inhibitor complex |
---|
機能・相同性 | 機能・相同性情報
receptor ligand inhibitor activity / HSP90-CDC37 chaperone complex / negative regulation of proteasomal protein catabolic process / Aryl hydrocarbon receptor signalling / aryl hydrocarbon receptor complex / dynein axonemal particle / histone methyltransferase binding / positive regulation of protein localization to cell surface / ATP-dependent protein binding / protein kinase regulator activity ...receptor ligand inhibitor activity / HSP90-CDC37 chaperone complex / negative regulation of proteasomal protein catabolic process / Aryl hydrocarbon receptor signalling / aryl hydrocarbon receptor complex / dynein axonemal particle / histone methyltransferase binding / positive regulation of protein localization to cell surface / ATP-dependent protein binding / protein kinase regulator activity / protein folding chaperone complex / telomerase holoenzyme complex assembly / Respiratory syncytial virus genome replication / Uptake and function of diphtheria toxin / TPR domain binding / positive regulation of transforming growth factor beta receptor signaling pathway / Assembly and release of respiratory syncytial virus (RSV) virions / dendritic growth cone / : / Sema3A PAK dependent Axon repulsion / regulation of protein ubiquitination / The NLRP3 inflammasome / telomere maintenance via telomerase / HSF1-dependent transactivation / response to unfolded protein / chaperone-mediated protein complex assembly / HSF1 activation / Attenuation phase / cellular response to interleukin-4 / RHOBTB2 GTPase cycle / axonal growth cone / Purinergic signaling in leishmaniasis infection / DNA polymerase binding / supramolecular fiber organization / chaperone-mediated protein folding / protein folding chaperone / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / nitric-oxide synthase regulator activity / ESR-mediated signaling / positive regulation of cell differentiation / ATP-dependent protein folding chaperone / peptide binding / DDX58/IFIH1-mediated induction of interferon-alpha/beta / tau protein binding / placenta development / Regulation of actin dynamics for phagocytic cup formation / kinase binding / histone deacetylase binding / Chaperone Mediated Autophagy / The role of GTSE1 in G2/M progression after G2 checkpoint / regulation of protein localization / disordered domain specific binding / positive regulation of nitric oxide biosynthetic process / double-stranded RNA binding / unfolded protein binding / melanosome / protein folding / MHC class II protein complex binding / cellular response to heat / secretory granule lumen / Estrogen-dependent gene expression / ficolin-1-rich granule lumen / Potential therapeutics for SARS / protein dimerization activity / protein stabilization / regulation of cell cycle / cadherin binding / neuronal cell body / ubiquitin protein ligase binding / Neutrophil degranulation / virion attachment to host cell / negative regulation of apoptotic process / protein kinase binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / perinuclear region of cytoplasm / cell surface / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / mitochondrion / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / identical protein binding / membrane / nucleus / plasma membrane / cytosol / cytoplasm類似検索 - 分子機能 Heat shock protein Hsp90, conserved site / Heat shock hsp90 proteins family signature. / HSP90, C-terminal domain / Heat shock protein Hsp90, N-terminal / Heat shock protein Hsp90 family / Hsp90 protein / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPase, C-terminal domain / Heat Shock Protein 90 / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase ...Heat shock protein Hsp90, conserved site / Heat shock hsp90 proteins family signature. / HSP90, C-terminal domain / Heat shock protein Hsp90, N-terminal / Heat shock protein Hsp90 family / Hsp90 protein / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPase, C-terminal domain / Heat Shock Protein 90 / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold / 2-Layer Sandwich / Alpha Beta類似検索 - ドメイン・相同性 |
---|
生物種 | Homo sapiens (ヒト) |
---|
手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 1.55390799533 Å |
---|
データ登録者 | Huck, J.D. / Que, N.L.S. / Gewirth, D.T. |
---|
資金援助 | 米国, 2件 組織 | 認可番号 | 国 |
---|
National Institutes of Health/National Cancer Institute (NIH/NCI) | P01CA186866 | 米国 | National Institutes of Health/National Cancer Institute (NIH/NCI) | R01CA095130 | 米国 |
|
---|
引用 | ジャーナル: Proteins / 年: 2019 タイトル: Structures of Hsp90 alpha and Hsp90 beta bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity. 著者: Huck, J.D. / Que, N.L.S. / Sharma, S. / Taldone, T. / Chiosis, G. / Gewirth, D.T. |
---|
履歴 | 登録 | 2018年11月30日 | 登録サイト: RCSB / 処理サイト: RCSB |
---|
改定 1.0 | 2019年7月3日 | Provider: repository / タイプ: Initial release |
---|
改定 1.1 | 2019年7月10日 | Group: Data collection / Database references / カテゴリ: citation / citation_author Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title |
---|
改定 1.2 | 2019年9月11日 | Group: Data collection / Database references / カテゴリ: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last |
---|
改定 1.3 | 2019年12月4日 | Group: Author supporting evidence / カテゴリ: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization |
---|
改定 1.4 | 2023年10月11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 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession |
---|
|
---|