|Entry||Database: PDB / ID: 1cmz|
|Title||SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING|
|Components||PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN)|
|Keywords||SIGNALING 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 species||Homo sapiens (human)|
|Method||SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING|
|Authors||De Alba, E. / De Vries, L. / Farquhar, M.G. / Tjandra, N.|
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.
|Structure viewer||Molecule: |
Downloads & links
A: PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN)
|#1: 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
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: TRIPLE-RESONANCE NMR SPECTROSCOPY USED ON 13C, 15N-LABELED GAIP|
|Details||Contents: 90% WATER/10% D2O, 100% D2O|
*PLUSMethod: other / Details: NMR
|NMR spectrometer||Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz|
|Refinement||Method: 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 ensemble||Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 167 / Conformers submitted total number: 20|
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