登録情報 データベース : PDB / ID : 1kn7 構造の表示 ダウンロードとリンクタイトル Solution structure of the tandem inactivation domain (residues 1-75) of potassium channel RCK4 (Kv1.4) 要素VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV1.4 詳細 キーワード MEMBRANE PROTEIN / voltage-gated potassium channel / inactivation domain / Kv1.4 / RCK4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
regulation of presynaptic membrane potential / Voltage gated Potassium channels / axon initial segment / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / voltage-gated potassium channel activity / action potential / potassium ion binding / potassium channel activity / asymmetric synapse ... regulation of presynaptic membrane potential / Voltage gated Potassium channels / axon initial segment / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / voltage-gated potassium channel activity / action potential / potassium ion binding / potassium channel activity / asymmetric synapse / voltage-gated potassium channel complex / potassium ion transmembrane transport / monoatomic ion transmembrane transport / potassium ion transport / dendritic shaft / protein homooligomerization / monoatomic ion channel activity / presynaptic membrane / postsynaptic membrane / dendritic spine / axon / glutamatergic synapse / cell surface / membrane / plasma membrane 類似検索 - 分子機能 Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4 / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain superfamily / Potassium channel Kv1.4 tandem inactivation domain / Potassium channel, voltage dependent, Kv1 / Potassium channel, voltage dependent, Kv / Potassium channel tetramerisation-type BTB domain / BTB/POZ domain / Broad-Complex, Tramtrack and Bric a brac ... Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain / Potassium channel, voltage dependent, Kv1.4 / Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain superfamily / Potassium channel Kv1.4 tandem inactivation domain / Potassium channel, voltage dependent, Kv1 / Potassium channel, voltage dependent, Kv / Potassium channel tetramerisation-type BTB domain / BTB/POZ domain / Broad-Complex, Tramtrack and Bric a brac / BTB/POZ domain / Voltage-dependent channel domain superfamily / SKP1/BTB/POZ domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Ion transport domain / Ion transport protein / Up-down Bundle / Mainly Alpha 類似検索 - ドメイン・相同性 Potassium voltage-gated channel subfamily A member 4 類似検索 - 構成要素生物種 Rattus norvegicus (ドブネズミ)手法 溶液NMR / simulated annealing , torsion angle dynamics 詳細データ登録者 Wissmann, R. / Bildl, W. / Oliver, D. / Beyermann, M. / Kalbitzer, H.R. / Bentrop, D. / Fakler, B. 引用ジャーナル : J.Biol.Chem. / 年 : 2003タイトル : Solution Structure and Function of the "Tandem Inactivation Domain" of the Neuronal A-type Potassium Channel Kv1.4著者 : Wissmann, R. / Bildl, W. / Oliver, D. / Beyermann, M. / Kalbitzer, H.R. / Bentrop, D. / Fakler, B. 履歴 登録 2001年12月18日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2003年5月6日 Provider : repository / タイプ : Initial release改定 1.1 2008年4月27日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Version format compliance改定 1.3 2022年2月23日 Group : Data collection / Database references / Derived calculationsカテゴリ : database_2 / pdbx_nmr_software ... database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model 改定 1.4 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 999 SEQUENCE The protein construct used in this study contains three additional residues at the N- ... SEQUENCE The protein construct used in this study contains three additional residues at the N-terminus from a thrombin cleavage site (Gly-Ser-Thr).