› 2msu

Solution NMR

NMR structure of Kindlin-2 F2 339-358

Released:
DOI: 10.2210/pdb2msu/pdb
PDB entry 2msu coloured by chain, ensemble of 19 models, front view.
PDB entry 2msu coloured by chain, ensemble of 19 models, side view.
PDB entry 2msu coloured by chain, ensemble of 19 models, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis of kindlin-2 binding to integrin-linked kinase pseudokinase for regulating cell adhesion.
Fukuda K, Bledzka K, Yang J, Perera HD, Plow EF, Qin J
J Biol Chem 289 28363-75 (2014)
PMID: 25160619

Function and Biology Details

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

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: 20 amino acids
Theoretical weight: 2.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96AC1 (Residues: 339-358; Coverage: 3%)
Gene names: FERMT2, KIND2, MIG2, PLEKHC1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 49%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Integrin activation by talin, kindlin and mechanical forces.
Sun et al. (2019)
8 more

1 mention without citation

Molecular basis of kindlin-2 binding to integrin-linked kinase pseudokinase for regulating cell adhesion.
Fukuda et al. (2014)