› 7m0g

Solid-state NMR

Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments

Released:
DOI: 10.2210/pdb7m0g/pdb
PDB entry 7m0g coloured by chain, ensemble of 10 models, front view.
PDB entry 7m0g coloured by chain, ensemble of 10 models, side view.
PDB entry 7m0g coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode.
Kraus J, Russell RW, Kudryashova E, Xu C, Katyal N, Perilla JR, Kudryashov DS, Polenova T
OpenAccess logo Nat Commun 13 2114 (2022)
PMID: 35440100

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195115 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cofilin-2 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y281 (Residues: 1-166; Coverage: 100%)
Gene name: CFL2
Sequence domains: Cofilin/tropomyosin-type actin-binding protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 40%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Actin Bundles Dynamics and Architecture.
Rajan et al. (2023)
1 more

1 mention without citation

Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode.
Kraus et al. (2022)

Experimental raw data

Links to raw experimental data available for this entry are listed below

NMR data related to PDB entry 7m0g available at Biological Magnetic Resonance Data Bank (BMRB)

BMRB accession: BMR30877

Available data:
  • Assigned chemical shifts: 1