› 4n1l

X-ray diffraction
1.99Å resolution

Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions

Released:
DOI: 10.2210/pdb4n1l/pdb
PDB entry 4n1l coloured by chain, front view.
PDB entry 4n1l coloured by chain, side view.
PDB entry 4n1l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.
Eibl C, Hessenberger M, Wenger J, Brandstetter H
Acta Crystallogr D Biol Crystallogr 70 2007-18 (2014)
PMID: 25004977

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NACHT, LRR and PYD domains-containing protein 14 Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 12.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86W24 (Residues: 1-100; Coverage: 9%)
Gene names: NALP14, NLRP14, NOD5
Sequence domains: PAAD/DAPIN/Pyrin domain
Structure domains: Death Domain, Fas

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21212
Unit cell:
a: 51.35Å b: 62.55Å c: 29.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Structural mechanisms in NLR inflammasome signaling.
Lechtenberg et al. (2014)
3 more

3 mentions without citation

Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond.
Ha et al. (2020)
2 more