› 1y3a

X-ray diffraction
2.5Å resolution

Structure of G-Alpha-I1 bound to a GDP-selective peptide provides insight into guanine nucleotide exchange

Released:
DOI: 10.2210/pdb1y3a/pdb
PDB entry 1y3a coloured by chain, front view.
PDB entry 1y3a coloured by chain, side view.
PDB entry 1y3a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange.
Johnston CA, Willard FS, Jezyk MR, Fredericks Z, Bodor ET, Jones MB, Blaesius R, Watts VJ, Harden TK, Sondek J, Ramer JK, Siderovski DP
Structure 13 1069-80 (2005)
PMID: 16004878

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158955 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Guanine nucleotide-binding protein G(i) subunit alpha-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 329 amino acids
Theoretical weight: 37.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63096 (Residues: 26-354; Coverage: 93%)
Gene name: GNAI1
Sequence domains: G-protein alpha subunit
Structure domains:
KB752 peptide Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 16 amino acids
Theoretical weight: 2.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand GDP 4 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 72.943Å b: 112.785Å c: 109.49Å
α: 90° β: 93.75° γ: 90°
R-values:
R R work R free
0.291 0.24 0.28
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

10 review citations

Heterotrimeric G protein activation by G-protein-coupled receptors.
Oldham et al. (2008)
9 more

22 mentions without citation

GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates Akt signaling.
Garcia-Marcos et al. (2009)
21 more