› 2lko

Solution NMR

Structural Basis of Phosphoinositide Binding to Kindlin-2 Pleckstrin Homology Domain in Regulating Integrin Activation

Released:
DOI: 10.2210/pdb2lko/pdb
PDB entry 2lko coloured by chain, ensemble of 20 models, front view.
PDB entry 2lko coloured by chain, ensemble of 20 models, side view.
PDB entry 2lko coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation.
Liu J, Fukuda K, Xu Z, Ma YQ, Hirbawi J, Mao X, Wu C, Plow EF, Qin J
J Biol Chem 286 43334-42 (2011)
PMID: 22030399

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fermitin family homolog 2 Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 15.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96AC1 (Residues: 367-500; Coverage: 20%)
Gene names: FERMT2, KIND2, MIG2, PLEKHC1
Sequence domains:
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 63%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Talins and kindlins: partners in integrin-mediated adhesion.
Calderwood et al. (2013)
15 more

5 mentions without citation

Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation.
Liu et al. (2011)
4 more