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- PDB-1bak: SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPL... -

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Entry
Database: PDB / ID: 1bak
TitleSIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPLED RECEPTOR KINASE 2 (BETA-ADRENERGIC RECEPTOR KINASE 1), C-TERMINAL EXTENDED, NMR, 20 STRUCTURES
ComponentsG-PROTEIN COUPLED RECEPTOR KINASE 2
KeywordsTRANSFERASE / 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


negative regulation of the force of heart contraction by chemical signal / negative regulation of relaxation of smooth muscle / beta-adrenergic-receptor kinase / Edg-2 lysophosphatidic acid receptor binding / alpha-2A adrenergic receptor binding / beta-adrenergic receptor kinase activity / G protein-coupled receptor kinase activity / tachykinin receptor signaling pathway / negative regulation of striated muscle contraction / positive regulation of catecholamine secretion ...negative regulation of the force of heart contraction by chemical signal / negative regulation of relaxation of smooth muscle / beta-adrenergic-receptor kinase / Edg-2 lysophosphatidic acid receptor binding / alpha-2A adrenergic receptor binding / beta-adrenergic receptor kinase activity / G protein-coupled receptor kinase activity / tachykinin receptor signaling pathway / negative regulation of striated muscle contraction / positive regulation of catecholamine secretion / desensitization of G protein-coupled receptor signaling pathway / Activation of SMO / cytoplasmic side of mitochondrial outer membrane / regulation of the force of heart contraction / Calmodulin induced events / cardiac muscle contraction / viral genome replication / G protein-coupled receptor binding / receptor internalization / G protein-coupled acetylcholine receptor signaling pathway / Cargo recognition for clathrin-mediated endocytosis / presynapse / heart development / G alpha (s) signalling events / G alpha (q) signalling events / protein kinase activity / postsynapse / cilium / G protein-coupled receptor signaling pathway / symbiont entry into host cell / ATP binding / membrane / plasma membrane / cytoplasm / cytosol
Similarity search - Function
GPCR kinase / Regulator of G protein signaling domain / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS, subdomain 2 / RGS domain superfamily / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / Extension to Ser/Thr-type protein kinases ...GPCR kinase / Regulator of G protein signaling domain / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS, subdomain 2 / RGS domain superfamily / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / PH domain / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / PH-like domain superfamily / Roll / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Beta
Similarity search - Domain/homology
Beta-adrenergic receptor kinase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / distance geometry
AuthorsFushman, 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
DepositionNov 21, 1997Processing site: BNL
Revision 1.0Feb 25, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / 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_database_status.process_site / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: G-PROTEIN COUPLED RECEPTOR KINASE 2


Theoretical massNumber of molelcules
Total (without water)14,2141
Polymers14,2141
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 400LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein G-PROTEIN COUPLED RECEPTOR KINASE 2 / GRK-2 / BETA-ADRENERGIC RECEPTOR KINASE 1 / BETA-ARK 1


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

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1111H-15N)HSQC
121(1H-13C)HSQC
131HSQC-J
141HTQC
1512D AND 3D 15N-NOESY-HMQC (IN H2O
161IN D2O) AND HOHAHA-HMQC
17113C-NOESY-HMQC
181(H)CCH-TOCSY
191CBCANH
1101CBCA(CO)NH
1111HNCA
1121HN(CO)CA
1131HNCO
1141{1H}15N-NOE
1151H2O-SELECTIVE 15N-EDITED NOESY AND ROESY
1161H-D-EXCHANGE

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Sample preparation

Sample conditionspH: 4.5 / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMX500BrukerDMX5005001
Bruker DMX600BrukerDMX6006002

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Processing

NMR software
NameClassification
XwinNMRstructure solution
XEASYstructure solution
DIANAstructure solution
DYANAstructure solution
DYANArefinement
RefinementMethod: distance geometry / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 400 / Conformers submitted total number: 20

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