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- PDB-1cmz: SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULA... -

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Basic information

Entry
Database: PDB / ID: 1cmz
TitleSOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING
ComponentsPROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN)
KeywordsSIGNALING PROTEIN REGULATION / GAIP / RGS / REGULATOR OF G PROTEIN
Function / homology
Function and homology information


clathrin-coated vesicle / small GTPase mediated signal transduction / brush border / G-protein alpha-subunit binding / negative regulation of signal transduction / G alpha (z) signalling events / autophagy / G alpha (i) signalling events / G alpha (q) signalling events / response to ethanol ...clathrin-coated vesicle / small GTPase mediated signal transduction / brush border / G-protein alpha-subunit binding / negative regulation of signal transduction / G alpha (z) signalling events / autophagy / G alpha (i) signalling events / G alpha (q) signalling events / response to ethanol / G protein-coupled receptor signaling pathway / membrane raft / Golgi apparatus / membrane / plasma membrane
Similarity search - Function
Regulator of G-protein Signalling 4; domain 1 - #10 / Regulator of G-protein Signalling 4; domain 1 / Regulator of G-protein Signalling 4, domain 2 / Regulator of G-protein Signalling 4; domain 2 / Regulator of G protein signaling domain / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Regulator of G-protein signaling 19
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsDe Alba, E. / De Vries, L. / Farquhar, M.G. / Tjandra, N.
Citation
Journal: J.Mol.Biol. / Year: 1999
Title: Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling.
Authors: de Alba, E. / De Vries, L. / Farquhar, M.G. / Tjandra, N.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1995
Title: GAIP, A Protein that Specifically Interacts with the Trimeric G Protein G(alphai3), is a Member of a Protein Family with a Highly Conserved Core Domain
Authors: De Vries, L. / Mousli, M. / Wurmser, A. / Farquhar, M.G.
History
DepositionMay 12, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Nov 10, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN)


Theoretical massNumber of molelcules
Total (without water)17,2861
Polymers17,2861
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 167LOWEST ENERGY
Representative

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Components

#1: Protein PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN) / GALPHA INTERACTING PROTEIN


Mass: 17286.326 Da / Num. of mol.: 1 / Fragment: RGS BOX
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX-2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P49795

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111CBCA(CO)NH
121CBCANH
131HBHA(CO)NH
141HNCA
151(H)CCH-TOCSY
161C-CNOESY
171N-CNOESY
181H-HNOESY
NMR detailsText: TRIPLE-RESONANCE NMR SPECTROSCOPY USED ON 13C, 15N-LABELED GAIP

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Sample preparation

DetailsContents: 90% WATER/10% D2O, 100% D2O
Sample conditions
Conditions-IDpHTemperature (K)
17.2 300 K
28.3 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
NMRPipestructure solution
PIPPstructure solution
X-PLORstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
Details: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136, USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE DIPOLAR ...Details: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136, USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE DIPOLAR COUPLING RESTRAINTS TJANDRA ET AL. (1997) NATURE STRUCT. BIOL. 4, 732-738.
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 167 / Conformers submitted total number: 20

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