登録情報 | データベース: PDB / ID: 2f2p |
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タイトル | Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode |
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要素 | Calmodulin fused with calmodulin-binding domain of calcineurin |
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キーワード | METAL BINDING PROTEIN / EF-hands / calcium / calmodulin / calcineurin |
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機能・相同性 | 機能・相同性情報
CLEC7A (Dectin-1) induces NFAT activation / Calcineurin activates NFAT / FCERI mediated Ca+2 mobilization / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of signaling / positive regulation of saliva secretion / calmodulin-dependent protein phosphatase activity / calcineurin complex / calcineurin-NFAT signaling cascade ...CLEC7A (Dectin-1) induces NFAT activation / Calcineurin activates NFAT / FCERI mediated Ca+2 mobilization / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of signaling / positive regulation of saliva secretion / calmodulin-dependent protein phosphatase activity / calcineurin complex / calcineurin-NFAT signaling cascade / renal filtration / positive regulation of osteoclast differentiation / Ca2+ pathway / myosin phosphatase activity / protein-serine/threonine phosphatase / positive regulation of ryanodine-sensitive calcium-release channel activity / positive regulation of activated T cell proliferation / negative regulation of ryanodine-sensitive calcium-release channel activity / epidermis development / positive regulation of osteoblast differentiation / skeletal muscle fiber development / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / dephosphorylation / keratinocyte differentiation / protein dephosphorylation / modulation of chemical synaptic transmission / sarcolemma / Z disc / spindle pole / response to calcium ion / dendritic spine / calmodulin binding / protein domain specific binding / calcium ion binding / protein-containing complex / metal ion binding / cytoplasm / cytosol類似検索 - 分子機能 PP2B, metallophosphatase domain / PP2B / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / EF-hand / Recoverin; domain 1 ...PP2B, metallophosphatase domain / PP2B / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / EF-hand / Recoverin; domain 1 / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Orthogonal Bundle / Mainly Alpha類似検索 - ドメイン・相同性 Calmodulin / Protein phosphatase 3 catalytic subunit alpha類似検索 - 構成要素 |
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生物種 | Bos taurus (ウシ) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.6 Å |
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データ登録者 | Ye, Q. / Wong, A. / Jia, Z. |
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引用 | ジャーナル: Biochemistry / 年: 2006 タイトル: Structure of calmodulin bound to a calcineurin Peptide: a new way of making an old binding mode. 著者: Ye, Q. / Li, X. / Wong, A. / Wei, Q. / Jia, Z. |
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履歴 | 登録 | 2005年11月17日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2006年2月21日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2008年5月1日 | Group: Version format compliance |
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改定 1.2 | 2011年7月13日 | Group: Version format compliance |
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改定 1.3 | 2017年8月2日 | Group: Refinement description / Source and taxonomy / カテゴリ: entity_src_gen / software |
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改定 1.4 | 2023年8月23日 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / 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 / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_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_seq_id |
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