› 3ixe

X-ray diffraction
1.9Å resolution

Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase

Released:
DOI: 10.2210/pdb3ixe/pdb
PDB entry 3ixe coloured by chain, front view.
PDB entry 3ixe coloured by chain, side view.
PDB entry 3ixe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase.
Chiswell BP, Stiegler AL, Razinia Z, Nalibotski E, Boggon TJ, Calderwood DA
J Struct Biol 170 157-63 (2010)
PMID: 19963065

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171668 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Integrin-linked protein kinase Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 20.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q13418 (Residues: 1-174; Coverage: 39%)
Gene names: ILK, ILK1, ILK2
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Ankyrin repeat-containing domain
LIM and senescent cell antigen-like-containing domain protein 2 Chain: B
Molecule details ›
Chain: B
Length: 72 amino acids
Theoretical weight: 8.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7Z4I7 (Residues: 11-73; Coverage: 19%)
Gene names: LIMS2, PINCH2
Sequence domains: LIM domain
Structure domains: Cysteine Rich Protein

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 41.416Å b: 72.01Å c: 83.937Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.22
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Chapter 22: Structural and signaling functions of integrins.
Kadry et al. (2020)
3 more

2 mentions without citation

Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase.
Chiswell et al. (2010)
1 more