登録情報 | データベース: PDB / ID: 1mhw |
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タイトル | Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides |
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要素 | - (Cathepsin L) x 2
- 4-biphenylacetyl-Cys-(D)Arg-Tyr-N-(2-phenylethyl) amide
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キーワード | HYDROLASE/HYDROLASE INHIBITOR / CATHEPSIN L / CYSTEINE PROTEASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX |
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機能・相同性 | 機能・相同性情報
enkephalin processing / cathepsin L / CD4-positive, alpha-beta T cell lineage commitment / macrophage apoptotic process / chromaffin granule / elastin catabolic process / antigen processing and presentation of peptide antigen / RUNX1 regulates transcription of genes involved in differentiation of keratinocytes / endolysosome lumen / cellular response to thyroid hormone stimulus ...enkephalin processing / cathepsin L / CD4-positive, alpha-beta T cell lineage commitment / macrophage apoptotic process / chromaffin granule / elastin catabolic process / antigen processing and presentation of peptide antigen / RUNX1 regulates transcription of genes involved in differentiation of keratinocytes / endolysosome lumen / cellular response to thyroid hormone stimulus / Trafficking and processing of endosomal TLR / zymogen activation / proteoglycan binding / Assembly of collagen fibrils and other multimeric structures / antigen processing and presentation / Collagen degradation / protein autoprocessing / collagen catabolic process / fibronectin binding / serpin family protein binding / collagen binding / Attachment and Entry / receptor-mediated endocytosis of virus by host cell / Degradation of the extracellular matrix / multivesicular body / endocytic vesicle lumen / MHC class II antigen presentation / cysteine-type peptidase activity / lysosomal lumen / proteolysis involved in protein catabolic process / Endosomal/Vacuolar pathway / antigen processing and presentation of exogenous peptide antigen via MHC class II / : / adaptive immune response / histone binding / Attachment and Entry / lysosome / apical plasma membrane / symbiont entry into host cell / fusion of virus membrane with host plasma membrane / cysteine-type endopeptidase activity / intracellular membrane-bounded organelle / fusion of virus membrane with host endosome membrane / Golgi apparatus / proteolysis / extracellular space / extracellular exosome / extracellular region / nucleus / plasma membrane類似検索 - 分子機能 Cysteine proteinases. Chain C / Cathepsin propeptide inhibitor domain (I29) / Cathepsin propeptide inhibitor domain (I29) / Cathepsin propeptide inhibitor domain (I29) / Papain-like cysteine endopeptidase / Cysteine peptidase, asparagine active site / Eukaryotic thiol (cysteine) proteases asparagine active site. / Cysteine peptidase, histidine active site / Eukaryotic thiol (cysteine) proteases histidine active site. / : ...Cysteine proteinases. Chain C / Cathepsin propeptide inhibitor domain (I29) / Cathepsin propeptide inhibitor domain (I29) / Cathepsin propeptide inhibitor domain (I29) / Papain-like cysteine endopeptidase / Cysteine peptidase, asparagine active site / Eukaryotic thiol (cysteine) proteases asparagine active site. / Cysteine peptidase, histidine active site / Eukaryotic thiol (cysteine) proteases histidine active site. / : / Peptidase C1A, papain C-terminal / Papain family cysteine protease / Papain family cysteine protease / Cysteine proteinases / Cysteine peptidase, cysteine active site / Eukaryotic thiol (cysteine) proteases cysteine active site. / Cathepsin B; Chain A / Papain-like cysteine peptidase superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Alpha-Beta Complex / Beta Barrel / Mainly Beta / Alpha Beta類似検索 - ドメイン・相同性 4-biphenylacetyl-CYS-(D)ARG-TYR-N-(2-phenylethyl) amide / Procathepsin L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 / 分子置換 / 解像度: 1.9 Å |
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データ登録者 | Chowdhury, S. / Sivaraman, J. / Wang, J. / Devanathan, G. / Lachance, P. / Qi, H. / Menard, R. / Lefebvre, J. / Konishi, Y. / Cygler, M. ...Chowdhury, S. / Sivaraman, J. / Wang, J. / Devanathan, G. / Lachance, P. / Qi, H. / Menard, R. / Lefebvre, J. / Konishi, Y. / Cygler, M. / Sulea, T. / Purisima, E.O. |
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引用 | ジャーナル: J.Med.Chem. / 年: 2002 タイトル: Design of non-covalent inhibitors of human cathepsin L. From the 96-residue proregion to optimized tripeptides 著者: Chowdhury, S. / Sivaraman, J. / Wang, J. / Devanathan, G. / Lachance, P. / Qi, H. / Menard, R. / Lefebvre, J. / Konishi, Y. / Cygler, M. / Sulea, T. / Purisima, E.O. |
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履歴 | 登録 | 2002年8月21日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2002年12月11日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2008年4月28日 | Group: Version format compliance |
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改定 1.2 | 2011年7月13日 | Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary / Version format compliance |
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改定 1.3 | 2012年12月12日 | Group: Other |
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改定 1.4 | 2014年11月19日 | Group: Non-polymer description |
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改定 1.5 | 2017年10月11日 | Group: Refinement description / カテゴリ: software |
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改定 1.6 | 2024年11月20日 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_initial_refinement_model / pdbx_modification_feature / struct_conn / 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_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_PDB_ins_code / _struct_conn.pdbx_ptnr2_PDB_ins_code / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_ins_code / _struct_site.pdbx_auth_seq_id |
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