› 5lxm

X-ray diffraction
2.08Å resolution

Crystal structure of Aurora-A bound to a hydrocarbon-stapled proteomimetic of TPX2

Released:
DOI: 10.2210/pdb5lxm/pdb
PDB entry 5lxm coloured by chain, front view.
PDB entry 5lxm coloured by chain, side view.
PDB entry 5lxm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A TPX2 Proteomimetic Has Enhanced Affinity for Aurora-A Due to Hydrocarbon Stapling of a Helix.
Rennie YK, McIntyre PJ, Akindele T, Bayliss R, Jamieson AG
ACS Chem Biol 11 3383-3390 (2016)
PMID: 27775325

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127236 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aurora kinase A Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 32.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14965 (Residues: 122-403; Coverage: 70%)
Gene names: AIK, AIRK1, ARK1, AURA, AURKA, AYK1, BTAK, IAK1, STK15, STK6
Sequence domains: Protein kinase domain
Structure domains:
Targeting protein for Xklp2 Chain: D
Molecule details ›
Chain: D
Length: 38 amino acids
Theoretical weight: 4.36 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9ULW0 (Residues: 6-43; Coverage: 5%)
Gene names: C20orf1, C20orf2, DIL2, HCA519, TPX2
Sequence domains: Aurora-A binding

Ligands and Environments

9 bound ligands:
Ligand ADP 1 x ADP
Ligand PG4 1 x PG4
Ligand SO4 1 x SO4
Ligand PEG 2 x PEG
Ligand MES 1 x MES
Ligand P4G 1 x P4G
Ligand CL 1 x CL
Ligand MG 2 x MG
Ligand NH3 1 x NH3
2 modified residues:
Ligand TPO 1 x TPO
Ligand MK8 2 x MK8

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3121
Unit cell:
a: 79.78Å b: 79.78Å c: 140.26Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.243
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Proteomimetics as protein-inspired scaffolds with defined tertiary folding patterns.
Horne et al. (2020)
2 more

5 mentions without citation

Stapled Peptides Inhibitors: A New Window for Target Drug Discovery.
Ali et al. (2019)
4 more