› 2lgx

Solution NMR

NMR structure for Kindle-2 N-terminus

Released:
DOI: 10.2210/pdb2lgx/pdb
PDB entry 2lgx coloured by chain, ensemble of 20 models, front view.
PDB entry 2lgx coloured by chain, ensemble of 20 models, side view.
PDB entry 2lgx coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation.
Perera HD, Ma YQ, Yang J, Hirbawi J, Plow EF, Qin J
Structure 19 1664-71 (2011)
PMID: 22078565

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: 112 amino acids
Theoretical weight: 12.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96AC1 (Residues: 1-105; Coverage: 15%)
Gene names: FERMT2, KIND2, MIG2, PLEKHC1
Sequence domains: Kindlin-2 N-terminal domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 78%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

3 mentions without citation

Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation.
Perera et al. (2011)
2 more