[English] 日本語
Yorodumi- PDB-1bak: SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bak | ||||||
---|---|---|---|---|---|---|---|
Title | SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPLED RECEPTOR KINASE 2 (BETA-ADRENERGIC RECEPTOR KINASE 1), C-TERMINAL EXTENDED, NMR, 20 STRUCTURES | ||||||
Components | G-PROTEIN COUPLED RECEPTOR KINASE 2 | ||||||
Keywords | TRANSFERASE / PLECKSTRIN HOMOLOGY DOMAIN / PH DOMAIN / SIGNAL TRANSDUCTION / G-BETA-GAMMA BINDING DOMAIN / BETA-ADRENERGIC RECEPTOR KINASE / BETA-ARK / G-PROTEIN COUPLED RECEPTOR KINASE (GRK-2) | ||||||
Function / homology | Function and homology information beta-adrenergic-receptor kinase / negative regulation of the force of heart contraction by chemical signal / negative regulation of relaxation of smooth muscle / beta-adrenergic receptor kinase activity / G protein-coupled receptor kinase activity / Edg-2 lysophosphatidic acid receptor binding / alpha-2A adrenergic receptor binding / positive regulation of catecholamine secretion / tachykinin receptor signaling pathway / Activation of SMO ...beta-adrenergic-receptor kinase / negative regulation of the force of heart contraction by chemical signal / negative regulation of relaxation of smooth muscle / beta-adrenergic receptor kinase activity / G protein-coupled receptor kinase activity / Edg-2 lysophosphatidic acid receptor binding / alpha-2A adrenergic receptor binding / positive regulation of catecholamine secretion / tachykinin receptor signaling pathway / Activation of SMO / negative regulation of striated muscle contraction / desensitization of G protein-coupled receptor signaling pathway / regulation of the force of heart contraction / Calmodulin induced events / cardiac muscle contraction / viral genome replication / G protein-coupled receptor binding / G protein-coupled acetylcholine receptor signaling pathway / cilium / receptor internalization / Cargo recognition for clathrin-mediated endocytosis / presynapse / heart development / G alpha (s) signalling events / postsynapse / G alpha (q) signalling events / peptidyl-serine phosphorylation / protein kinase activity / symbiont entry into host cell / G protein-coupled receptor signaling pathway / ATP binding / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Fushman, D. / Cowburn, D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1998 Title: The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. Authors: Fushman, D. / Najmabadi-Haske, T. / Cahill, S. / Zheng, J. / LeVine 3rd., H. / Cowburn, D. #1: Journal: Biochemistry / Year: 1995 Title: Structural Studies on the Ph Domains of Dbl, SOS1, Irs-1, and Beta Ark1 and Their Differential Binding to G Beta Gamma Subunits Authors: Mahadevan, D. / Thanki, N. / Singh, J. / Mcphie, P. / Zangrilli, D. / Wang, L.M. / Guerrero, C. / Levine III, H. / Humblet, C. / Saldanha, J. / Gutkind, J.S. / Najmabadi-Haske, T. #2: Journal: J.Biol.Chem. / Year: 1994 Title: Binding of G Protein Beta Gamma-Subunits to Pleckstrin Homology Domains Authors: Touhara, K. / Inglese, J. / Pitcher, J.A. / Shaw, G. / Lefkowitz, R.J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1bak.cif.gz | 775.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1bak.ent.gz | 672.4 KB | Display | PDB format |
PDBx/mmJSON format | 1bak.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ba/1bak ftp://data.pdbj.org/pub/pdb/validation_reports/ba/1bak | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 14214.492 Da / Num. of mol.: 1 / Fragment: C-TERMINAL EXTENDED PLECKSTRIN HOMOLOGY DOMAIN / Mutation: D552G, Y553S, A554H, L555M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P25098, EC: 2.7.1.126 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Sample conditions | pH: 4.5 / Temperature: 308 K |
---|---|
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: distance geometry / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 400 / Conformers submitted total number: 20 |