登録情報 データベース : PDB / ID : 2be6 構造の表示 ダウンロードとリンクタイトル 2.0 A crystal structure of the CaV1.2 IQ domain-Ca/CaM complex 要素Calmodulin 2 Voltage-dependent L-type calcium channel alpha-1C subunit 詳細キーワード MEMBRANE PROTEIN / calmodulin / calcium channel / IQ domain / inactivation / facilitation / calcium-dependent / gating / voltage-gated機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
Wnt signaling pathway, calcium modulating pathway / voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / regulation of high voltage-gated calcium channel activity / immune system development / positive regulation of adenylate cyclase activity / inositol phosphate metabolic process / membrane depolarization during atrial cardiac muscle cell action potential / regulation of opsin-mediated signaling pathway / Phase 2 - plateau phase ... Wnt signaling pathway, calcium modulating pathway / voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / regulation of high voltage-gated calcium channel activity / immune system development / positive regulation of adenylate cyclase activity / inositol phosphate metabolic process / membrane depolarization during atrial cardiac muscle cell action potential / regulation of opsin-mediated signaling pathway / Phase 2 - plateau phase / calcium ion transmembrane transport via high voltage-gated calcium channel / platelet degranulation / regulation of nitric-oxide synthase activity / membrane depolarization during AV node cell action potential / high voltage-gated calcium channel activity / : / : / positive regulation of cyclic-nucleotide phosphodiesterase activity / cardiac conduction / L-type voltage-gated calcium channel complex / : / membrane depolarization during cardiac muscle cell action potential / positive regulation of muscle contraction / negative regulation of peptidyl-threonine phosphorylation / cell communication by electrical coupling involved in cardiac conduction / regulation of ventricular cardiac muscle cell action potential / establishment of protein localization to mitochondrial membrane / NCAM1 interactions / camera-type eye development / cardiac muscle cell action potential involved in contraction / type 3 metabotropic glutamate receptor binding / embryonic forelimb morphogenesis / calcium ion transport into cytosol / glycogen catabolic process / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / positive regulation of peptidyl-threonine phosphorylation / positive regulation of ryanodine-sensitive calcium-release channel activity / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / positive regulation of DNA binding / voltage-gated calcium channel complex / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / CaMK IV-mediated phosphorylation of CREB / PKA activation / negative regulation of high voltage-gated calcium channel activity / Glycogen breakdown (glycogenolysis) / CLEC7A (Dectin-1) induces NFAT activation / response to corticosterone / Activation of RAC1 downstream of NMDARs / organelle localization by membrane tethering / negative regulation of ryanodine-sensitive calcium-release channel activity / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / negative regulation of calcium ion export across plasma membrane / regulation of cardiac muscle cell action potential / presynaptic endocytosis / nitric-oxide synthase binding / Synthesis of IP3 and IP4 in the cytosol / regulation of cell communication by electrical coupling involved in cardiac conduction / Phase 0 - rapid depolarisation / Fc-epsilon receptor signaling pathway / calcineurin-mediated signaling / Negative regulation of NMDA receptor-mediated neuronal transmission / regulation of synaptic vesicle exocytosis / Unblocking of NMDA receptors, glutamate binding and activation / alpha-actinin binding / positive regulation of protein autophosphorylation / RHO GTPases activate PAKs / regulation of heart rate by cardiac conduction / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / regulation of ryanodine-sensitive calcium-release channel activity / calcium ion import across plasma membrane / Long-term potentiation / protein phosphatase activator activity / Calcineurin activates NFAT / adenylate cyclase binding / Regulation of MECP2 expression and activity / DARPP-32 events / catalytic complex / Smooth Muscle Contraction / regulation of synaptic vesicle endocytosis / detection of calcium ion / regulation of cardiac muscle contraction / viral process / positive regulation of protein serine/threonine kinase activity / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / voltage-gated calcium channel activity / calcium channel inhibitor activity / cellular response to interferon-beta / activation of adenylate cyclase activity / Protein methylation / presynaptic cytosol / Activation of AMPK downstream of NMDARs 類似検索 - 分子機能 Calmodulin / Voltage-dependent calcium channel, L-type, alpha-1C subunit / Voltage-gated calcium channel subunit alpha, C-terminal / Voltage-gated calcium channel subunit alpha, C-term / Voltage-dependent calcium channel, L-type, alpha-1 subunit / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Voltage-dependent calcium channel, alpha-1 subunit / Voltage-dependent L-type calcium channel, IQ-associated domain ... Calmodulin / Voltage-dependent calcium channel, L-type, alpha-1C subunit / Voltage-gated calcium channel subunit alpha, C-terminal / Voltage-gated calcium channel subunit alpha, C-term / Voltage-dependent calcium channel, L-type, alpha-1 subunit / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Voltage-dependent calcium channel, alpha-1 subunit / Voltage-dependent L-type calcium channel, IQ-associated domain / Voltage-dependent L-type calcium channel, IQ-associated / : / Voltage-dependent channel domain superfamily / 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 / Ion transport domain / Ion transport protein / EF-hand domain pair / Orthogonal Bundle / Mainly Alpha 類似検索 - ドメイン・相同性 NICKEL (II) ION / Calmodulin-1 / Voltage-dependent L-type calcium channel subunit alpha-1C / Voltage-dependent L-type calcium channel subunit alpha-1C / Calmodulin-1 類似検索 - 構成要素生物種 Homo sapiens (ヒト)手法 X線回折 / シンクロトロン / 多波長異常分散 / 解像度 : 2 Å 詳細データ登録者 Van Petegem, F. / Chatelain, F.C. / Minor Jr., D.L. 引用ジャーナル : Nat.Struct.Mol.Biol. / 年 : 2005タイトル : Insights into voltage-gated calcium channel regulation from the structure of the Ca(V)1.2 IQ domain-Ca(2+)/calmodulin complex著者 : van Petegem, F. / Chatelain, F.C. / Minor Jr., D.L. 履歴 登録 2005年10月23日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2005年11月15日 Provider : repository / タイプ : Initial release改定 1.1 2008年5月1日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Advisory / Version format compliance改定 1.3 2017年10月18日 Group : Refinement description / カテゴリ : software改定 1.4 2022年12月21日 Group : Database references / Derived calculationsカテゴリ : database_2 / pdbx_struct_conn_angle ... database_2 / 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_alt_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.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_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.pdbx_ptnr1_label_alt_id / _struct_conn.pdbx_ptnr2_label_alt_id / _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_atom_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_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 改定 1.5 2024年5月22日 Group : Data collection / カテゴリ : chem_comp_atom / chem_comp_bond
すべて表示 表示を減らす Remark 600 HETEROGEN Calcium 501, 502, 503, 504 are associated with chain A, Ca 506, 507, 508, 509 with chain ... HETEROGEN Calcium 501, 502, 503, 504 are associated with chain A, Ca 506, 507, 508, 509 with chain B and Ca 511, 512, 513, 514 with chain C. Ni 505 is associated with chain A, 510 with chain B and 515 with chain C.