0000000001299156

AUTHOR

Eike Staub

showing 2 related works from this author

The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition.

2003

The PYRIN domain is a conserved sequence motif identified in more than 20 human proteins with putative functions in apoptotic and inflammatory signalling pathways. The three-dimensional structure of the PYRIN domain from human ASC was determined by NMR spectroscopy. The structure determination reveals close structural similarity to death domains, death effector domains, and caspase activation and recruitment domains, although the structural alignment with these other members of the death-domain superfamily differs from previously predicted amino acid sequence alignments. Two highly positively and negatively charged surfaces in the PYRIN domain of ASC result in a strong electrostatic dipole …

Models MolecularProtein FoldingMagnetic Resonance SpectroscopyCARD Signaling Adaptor ProteinsProtein ConformationProtein domainMolecular Sequence DataStatic ElectricityBiologyPyrin domainProtein Structure SecondaryConserved sequenceProtein structureStructural BiologyAnimalsHumansAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceZebrafishDeath domainGeneticsModels StatisticalSequence Homology Amino AcidProteinsPyrinZebrafish ProteinsCell biologyProtein Structure TertiaryCARD Signaling Adaptor ProteinsCytoskeletal ProteinsSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProtein foldingProtein BindingSignal TransductionJournal of molecular biology
researchProduct

nmr structure of the pyrin domain of human asc

2022

researchProduct