登録情報 | データベース: PDB / ID: 4i1r |
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タイトル | Human MALT1 (caspase-IG3) in complex with thioridazine |
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要素 | Mucosa-associated lymphoid tissue lymphoma translocation protein 1 |
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キーワード | HYDROLASE/HYDROLASE INHIBITOR / protease / HYDROLASE-HYDROLASE INHIBITOR complex |
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機能・相同性 | 機能・相同性情報
polkadots / B-1 B cell differentiation / positive regulation of T-helper 17 cell differentiation / CBM complex / regulation of T cell receptor signaling pathway / response to fungus / activation of NF-kappaB-inducing kinase activity / CLEC7A/inflammasome pathway / nuclear export / B cell activation ...polkadots / B-1 B cell differentiation / positive regulation of T-helper 17 cell differentiation / CBM complex / regulation of T cell receptor signaling pathway / response to fungus / activation of NF-kappaB-inducing kinase activity / CLEC7A/inflammasome pathway / nuclear export / B cell activation / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / small molecule binding / T cell proliferation / lipopolysaccharide-mediated signaling pathway / positive regulation of interleukin-2 production / proteolysis involved in protein catabolic process / positive regulation of interleukin-1 beta production / positive regulation of protein ubiquitination / Activation of NF-kappaB in B cells / positive regulation of T cell cytokine production / CLEC7A (Dectin-1) signaling / fibrillar center / defense response / FCERI mediated NF-kB activation / ubiquitin-protein transferase activity / : / Downstream TCR signaling / peptidase activity / positive regulation of NF-kappaB transcription factor activity / T cell receptor signaling pathway / regulation of apoptotic process / positive regulation of canonical NF-kappaB signal transduction / protease binding / endopeptidase activity / 加水分解酵素; プロテアーゼ; ペプチド結合加水分解酵素; システインプロテアーゼ / cysteine-type endopeptidase activity / innate immune response / negative regulation of apoptotic process / perinuclear region of cytoplasm / protein-containing complex / proteolysis / identical protein binding / nucleus / cytoplasm / cytosol類似検索 - 分子機能 Immunoglobulin-like - #3360 / Mucosa-associated lymphoid tissue lymphoma translocation protein 1 / MALT1, death domain / MALT1 immunoglobulin-like domain / MALT1 Ig-like domain / Rossmann fold - #1460 / Immunoglobulin domain / Peptidase C14, p20 domain / Caspase family p20 domain profile. / : ...Immunoglobulin-like - #3360 / Mucosa-associated lymphoid tissue lymphoma translocation protein 1 / MALT1, death domain / MALT1 immunoglobulin-like domain / MALT1 Ig-like domain / Rossmann fold - #1460 / Immunoglobulin domain / Peptidase C14, p20 domain / Caspase family p20 domain profile. / : / Caspase domain / Caspase-like domain superfamily / Immunoglobulin domain / Death-like domain superfamily / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta類似検索 - ドメイン・相同性 Chem-LZU / Mucosa-associated lymphoid tissue lymphoma translocation protein 1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: 2.7 Å |
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データ登録者 | Schlauderer, F. / Lammens, K. / Hopfner, K.P. |
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引用 | ジャーナル: Angew.Chem.Int.Ed.Engl. / 年: 2013 タイトル: Structural Analysis of Phenothiazine Derivatives as Allosteric Inhibitors of the MALT1 Paracaspase. 著者: Schlauderer, F. / Lammens, K. / Nagel, D. / Vincendeau, M. / Eitelhuber, A.C. / Verhelst, S.H. / Kling, D. / Chrusciel, A. / Ruland, J. / Krappmann, D. / Hopfner, K.P. |
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履歴 | 登録 | 2012年11月21日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2013年8月28日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2013年10月16日 | Group: Database references |
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改定 1.2 | 2024年2月28日 | Group: Data collection / Database references / Derived calculations カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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