› 1ucp

Solution NMR

NMR structure of the PYRIN domain of human ASC

Released:
DOI: 10.2210/pdb1ucp/pdb
PDB entry 1ucp coloured by chain, ensemble of 20 models, front view.
PDB entry 1ucp coloured by chain, ensemble of 20 models, side view.
PDB entry 1ucp coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition.
Liepinsh E, Barbals R, Dahl E, Sharipo A, Staub E, Otting G
J Mol Biol 332 1155-63 (2003)
PMID: 14499617

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apoptosis-associated speck-like protein containing a CARD Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 10.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ULZ3 (Residues: 1-91; Coverage: 47%)
Gene names: ASC, CARD5, PYCARD, TMS1
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
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

40 review citations

NOD-LRR proteins: role in host-microbial interactions and inflammatory disease.
Inohara et al. (2005)
39 more

23 mentions without citation

Inhibiting the inflammasome: one domain at a time.
Dorfleutner et al. (2015)
22 more