› 4x1l

X-ray diffraction
2.16Å resolution

Structural basis for mutation-induced destabilization of Profilin 1 in ALS

Released:
DOI: 10.2210/pdb4x1l/pdb
PDB entry 4x1l coloured by chain, front view.
PDB entry 4x1l coloured by chain, side view.
PDB entry 4x1l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for mutation-induced destabilization of profilin 1 in ALS.
Boopathy S, Silvas TV, Tischbein M, Jansen S, Shandilya SM, Zitzewitz JA, Landers JE, Goode BL, Schiffer CA, Bosco DA
Proc Natl Acad Sci U S A 112 7984-9 (2015)
PMID: 26056300

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-139726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Profilin-1 Chain: A
Molecule details ›
Chain: A
Length: 140 amino acids
Theoretical weight: 15.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07737 (Residues: 1-140; Coverage: 100%)
Gene name: PFN1
Sequence domains: Profilin
Structure domains: Dynein light chain 2a, cytoplasmic

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 74.26Å b: 31.84Å c: 61.02Å
α: 90° β: 122.66° γ: 90°
R-values:
R R work R free
0.217 0.216 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

The Actin Cytoskeleton in SMA and ALS: How Does It Contribute to Motoneuron Degeneration?
Hensel et al. (2018)
8 more

3 mentions without citation

Profilin1 biology and its mutation, actin(g) in disease.
Alkam et al. (2017)
2 more