+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2drn | ||||||
---|---|---|---|---|---|---|---|
タイトル | Docking and dimerization domain (D/D) of the Type II-alpha regulatory subunity of protein kinase A (PKA) in complex with a peptide from an A-kinase anchoring protein | ||||||
要素 |
| ||||||
キーワード | TRANSFERASE / AKAP / PKA / signal transduction / 4-helix bundle / helix-loop-helix / protein-peptide complex | ||||||
機能・相同性 | 機能・相同性情報 regulation of sarcomere organization / PKA activation in glucagon signalling / CREB1 phosphorylation through the activation of Adenylate Cyclase / GPER1 signaling / DARPP-32 events / Factors involved in megakaryocyte development and platelet production / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / Hedgehog 'off' state / PKA activation / negative regulation of cAMP/PKA signal transduction ...regulation of sarcomere organization / PKA activation in glucagon signalling / CREB1 phosphorylation through the activation of Adenylate Cyclase / GPER1 signaling / DARPP-32 events / Factors involved in megakaryocyte development and platelet production / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / Hedgehog 'off' state / PKA activation / negative regulation of cAMP/PKA signal transduction / cAMP-dependent protein kinase regulator activity / nucleotide-activated protein kinase complex / MAP-kinase scaffold activity / cardiac muscle cell differentiation / regulation of Rho protein signal transduction / Vasopressin regulates renal water homeostasis via Aquaporins / regulation of small GTPase mediated signal transduction / cAMP-dependent protein kinase inhibitor activity / beta-2 adrenergic receptor binding / cAMP-dependent protein kinase complex / protein kinase A binding / NRAGE signals death through JNK / positive regulation of Rho protein signal transduction / RHOB GTPase cycle / small molecule binding / adrenergic receptor signaling pathway / RHOC GTPase cycle / plasma membrane raft / protein kinase A catalytic subunit binding / axoneme / RHOA GTPase cycle / cAMP binding / T-tubule / guanyl-nucleotide exchange factor activity / bone development / regulation of protein phosphorylation / modulation of chemical synaptic transmission / small GTPase binding / G alpha (12/13) signalling events / heart development / cell cortex / positive regulation of canonical NF-kappaB signal transduction / molecular adaptor activity / G protein-coupled receptor signaling pathway / protein domain specific binding / centrosome / glutamatergic synapse / ubiquitin protein ligase binding / synapse / protein-containing complex binding / perinuclear region of cytoplasm / protein-containing complex / identical protein binding / membrane / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | Rattus norvegicus (ドブネズミ) | ||||||
手法 | 溶液NMR / simulated annealing | ||||||
データ登録者 | Newlon, M.G. / Roy, M. / Morikis, D. / Hausken, Z.E. / Coghlan, V. / Scott, J.D. / Jennings, P.A. | ||||||
引用 | ジャーナル: Embo J. / 年: 2001 タイトル: A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. 著者: Newlon, M.G. / Roy, M. / Morikis, D. / Carr, D.W. / Westphal, R. / Scott, J.D. / Jennings, P.A. | ||||||
履歴 |
|
-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
---|
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 2drn.cif.gz | 427.8 KB | 表示 | PDBx/mmCIF形式 |
---|---|---|---|---|
PDB形式 | pdb2drn.ent.gz | 361.2 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2drn.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 2drn_validation.pdf.gz | 368.1 KB | 表示 | wwPDB検証レポート |
---|---|---|---|---|
文書・詳細版 | 2drn_full_validation.pdf.gz | 627.2 KB | 表示 | |
XML形式データ | 2drn_validation.xml.gz | 26.5 KB | 表示 | |
CIF形式データ | 2drn_validation.cif.gz | 43.7 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/dr/2drn ftp://data.pdbj.org/pub/pdb/validation_reports/dr/2drn | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR アンサンブル |
|
-要素
#1: タンパク質・ペプチド | 分子量: 5398.181 Da / 分子数: 2 断片: N-terminal docking and dimerization domain, residues 4-46 由来タイプ: 組換発現 / 由来: (組換発現) Rattus norvegicus (ドブネズミ) / 遺伝子: RIIA(1-44) / プラスミド: PET-16B / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P12368, EC: 2.7.1.37 #2: タンパク質・ペプチド | | 分子量: 2533.828 Da / 分子数: 1 / 由来タイプ: 合成 詳細: The peptide has been generated by solid phase peptide synthesis.; This sequence occurs naturally in humans. 参照: UniProt: Q14572, UniProt: Q12802*PLUS |
---|
-実験情報
-実験
実験 | 手法: 溶液NMR |
---|---|
NMR実験の詳細 | Text: This structure was determined using standard 2d and 3d heteronuclear and homonuclear techniques. |
-試料調製
詳細 | 内容: 2mM RII-alpha(1-44); 90% H2O, 10% D2O / 溶媒系: 90% H2O/10% D2O |
---|---|
試料状態 | pH: 4 / 圧: 1 atm / 温度: 298 K |
-NMR測定
NMRスペクトロメーター | タイプ: Bruker DMX / 製造業者: Bruker / モデル: DMX / 磁場強度: 500 MHz |
---|
-解析
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
精密化 | 手法: simulated annealing / ソフトェア番号: 1 詳細: The structures are based on a total of 1370 restraints, 1247 are noe-derived distance restraints, 50 dihedral angle restraints,73 distance restraints from hydrogen bonds. | ||||||||||||
代表構造 | 選択基準: lowest energy | ||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 50 / 登録したコンフォーマーの数: 13 |