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Solution NMR

SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING

Released:
DOI: 10.2210/pdb1cmz/pdb
PDB entry 1cmz coloured by chain, ensemble of 20 models, front view.
PDB entry 1cmz coloured by chain, ensemble of 20 models, side view.
PDB entry 1cmz coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling.
de Alba E, De Vries L, Farquhar MG, Tjandra N
J Mol Biol 291 927-39 (1999)
PMID: 10452897

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156045 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Regulator of G-protein signaling 19 Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49795 (Residues: 79-214; Coverage: 63%)
Gene names: GAIP, GNAI3IP, RGS19
Sequence domains: Regulator of G protein signaling domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY, SIMULATED ANNEALING
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins.
Ross et al. (2000)
9 more

13 mentions without citation

Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits.
Soundararajan et al. (2008)
12 more