登録情報 | データベース: PDB / ID: 4v0c |
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タイトル | Crystal Structure of the Kv7.1 proximal C-terminal Domain in Complex with Calmodulin |
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要素 | - CALMODULIN
- POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 1
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キーワード | SIGNALING PROTEIN / VOLTAGE-DEPENDENT POTASSIUM CHANNELS / LONG QT SYNDROME / CALMODULIN |
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機能・相同性 | 機能・相同性情報
gastrin-induced gastric acid secretion / corticosterone secretion / voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization / basolateral part of cell / lumenal side of membrane / negative regulation of voltage-gated potassium channel activity / rhythmic behavior / iodide transport / regulation of gastric acid secretion / stomach development ...gastrin-induced gastric acid secretion / corticosterone secretion / voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization / basolateral part of cell / lumenal side of membrane / negative regulation of voltage-gated potassium channel activity / rhythmic behavior / iodide transport / regulation of gastric acid secretion / stomach development / voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization / membrane repolarization during atrial cardiac muscle cell action potential / Phase 3 - rapid repolarisation / membrane repolarization during action potential / regulation of atrial cardiac muscle cell membrane repolarization / Phase 2 - plateau phase / intracellular chloride ion homeostasis / membrane repolarization during ventricular cardiac muscle cell action potential / membrane repolarization during cardiac muscle cell action potential / negative regulation of delayed rectifier potassium channel activity / renal sodium ion absorption / detection of mechanical stimulus involved in sensory perception of sound / auditory receptor cell development / potassium ion export across plasma membrane / atrial cardiac muscle cell action potential / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / regulation of membrane repolarization / protein phosphatase 1 binding / : / : / positive regulation of cyclic-nucleotide phosphodiesterase activity / : / establishment of protein localization to mitochondrial membrane / delayed rectifier potassium channel activity / negative regulation of peptidyl-threonine phosphorylation / type 3 metabotropic glutamate receptor binding / positive regulation of potassium ion transmembrane transport / ventricular cardiac muscle cell action potential / Voltage gated Potassium channels / potassium ion homeostasis / non-motile cilium assembly / regulation of ventricular cardiac muscle cell membrane repolarization / cardiac muscle cell contraction / outward rectifier potassium channel activity / CaM pathway / intestinal absorption / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / inner ear morphogenesis / positive regulation of DNA binding / PKA activation / CaMK IV-mediated phosphorylation of CREB / negative regulation of high voltage-gated calcium channel activity / response to corticosterone / positive regulation of peptidyl-threonine phosphorylation / Glycogen breakdown (glycogenolysis) / CLEC7A (Dectin-1) induces NFAT activation / Activation of RAC1 downstream of NMDARs / nitric-oxide synthase binding / negative regulation of calcium ion export across plasma membrane / organelle localization by membrane tethering / mitochondrion-endoplasmic reticulum membrane tethering / adrenergic receptor signaling pathway / autophagosome membrane docking / regulation of synaptic vesicle exocytosis / cochlea development / presynaptic endocytosis / renal absorption / regulation of heart contraction / regulation of cardiac muscle cell action potential / ciliary base / positive regulation of ryanodine-sensitive calcium-release channel activity / Synthesis of IP3 and IP4 in the cytosol / protein kinase A regulatory subunit binding / regulation of cell communication by electrical coupling involved in cardiac conduction / Phase 0 - rapid depolarisation / protein kinase A catalytic subunit binding / Negative regulation of NMDA receptor-mediated neuronal transmission / negative regulation of ryanodine-sensitive calcium-release channel activity / social behavior / potassium ion import across plasma membrane / Unblocking of NMDA receptors, glutamate binding and activation / RHO GTPases activate PAKs / calcineurin-mediated signaling / inner ear development / regulation of heart rate by cardiac conduction / regulation of synaptic vesicle endocytosis / Ion transport by P-type ATPases / positive regulation of protein autophosphorylation / Uptake and function of anthrax toxins / action potential / Long-term potentiation / Regulation of MECP2 expression and activity / Calcineurin activates NFAT類似検索 - 分子機能 Potassium channel, voltage dependent, KCNQ1 / Potassium channel, voltage dependent, KCNQ / Potassium channel, voltage dependent, KCNQ, C-terminal / KCNQ voltage-gated potassium channel / Voltage-dependent channel domain superfamily / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. ...Potassium channel, voltage dependent, KCNQ1 / Potassium channel, voltage dependent, KCNQ / Potassium channel, voltage dependent, KCNQ, C-terminal / KCNQ voltage-gated potassium channel / Voltage-dependent channel domain superfamily / : / 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 / Ion transport domain / Ion transport protein / EF-hand domain pair類似検索 - ドメイン・相同性 THIOCYANATE ION / Calmodulin-1 / Potassium voltage-gated channel subfamily KQT member 1 / Calmodulin-3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 / 多波長異常分散 / 解像度: 2.86 Å |
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データ登録者 | Sachyani, D. / Hirsch, J.A. |
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引用 | ジャーナル: Structure / 年: 2014 タイトル: Structural Basis of a Kv7.1 Potassium Channel Gating Module: Studies of the Intracellular C-Terminal Domain in Complex with Calmodulin. 著者: Sachyani, D. / Dvir, M. / Strulovich, R. / Tria, G. / Tobelaim, W. / Peretz, A. / Pongs, O. / Svergun, D. / Attali, B. / Hirsch, J.A. |
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履歴 | 登録 | 2014年9月14日 | 登録サイト: PDBE / 処理サイト: PDBE |
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改定 1.0 | 2014年11月5日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2014年12月17日 | Group: Database references |
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改定 1.2 | 2024年5月8日 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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_asym_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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