Mapping of the ligand-binding site on the b ' domain of human PDI: interaction with peptide ligands and the x-linker region [PDF]
, 2009 PDI (protein disulfide-isomerase) catalyses the formation of native disulfide bonds of secretory proteins in the endoplasmic reticulum. PDI consists of four thioredoxin-like domains, of which two contain redox-active catalytic sites (a and a'), and two ...
Freedman, R. B. +15 more
core +1 more source
Structural and functional characterization of mature forms of metalloprotease E495 from Arctic sea-ice bacterium Pseudoalteromonas sp. SM495. [PDF]
PLoS ONE, 2012 E495 is the most abundant protease secreted by the Arctic sea-ice bacterium Pseudoalteromonas sp. SM495. As a thermolysin family metalloprotease, E495 was found to have multiple active forms in the culture of strain SM495.
Hai-Lun He +8 more
doaj +1 more source
Tetrameric Structure of a Serine Integrase Catalytic Domain [PDF]
Structure, 2008 The serine integrases have recently emerged as powerful new chromosome engineering tools in various organisms and show promise for therapeutic use in human cells. The serine integrases are structurally and mechanistically unrelated to the bacteriophage lambda integrase but share a similar catalytic domain with the resolvase/invertase enzymes typified ...
Yuan, Peng +2 more
openaire +2 more sources
The catalytic residues of Tn3 resolvase [PDF]
, 2009 To characterize the residues that participate in the catalysis of DNA cleavage and rejoining by the site-specific recombinase Tn3 resolvase, we mutated conserved polar or charged residues in the catalytic domain of an activated resolvase variant.
Olorunniji, F.J. +5 more
core +1 more source
A Monoclonal Antibody Against the Catalytic Domain of PTP1B [PDF]
Hybridoma, 2012 Protein tyrosine phosphatase 1B (PTP1B), a member of the protein tyrosine phosphatase (PTP) family, plays a crucial role in metabolic signaling, with insulin and leptin signaling being well studied. New evidence indicates that PTP1B is also involved in cancer.
Zeng, Fanwei +9 more
openaire +3 more sources
Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4 [PDF]
, 2018 Mucin-type O-glycosylation is initiated by a family of polypeptide GalNAc-transferases (GalNAc-Ts) which are type-II transmembrane proteins that contain Golgi luminal catalytic and lectin domains that are connected by a flexible linker. Several GalNAc-Ts,
Lluis Raich +52 more
core +1 more source
The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain [PDF]
, 2010 This work was funded by the Scottish Universities Life Sciences Alliance (SULSA).Primase and GINS are essential factors for chromosomal DNA replication in eukaryotic and archaeal cells.
Agnieszka Swiatek +5 more
core +1 more source
Hybrid and rogue kinases encoded in the genomes of model eukaryotes. [PDF]
PLoS ONE, 2014 The highly modular nature of protein kinases generates diverse functional roles mediated by evolutionary events such as domain recombination, insertion and deletion of domains.
Ramaswamy Rakshambikai +2 more
doaj +1 more source
Structural Complementation of the Catalytic Domain of Pseudomonas Exotoxin A [PDF]
Journal of Molecular Biology, 2014 The catalytic moiety of Pseudomonas exotoxin A (domain III or PE3) inhibits protein synthesis by ADP-ribosylation of eukaryotic elongation factor 2. PE3 is widely used as a cytocidal payload in receptor-targeted protein toxin conjugates. We have designed and characterized catalytically inactive fragments of PE3 that are capable of structural ...
Boland, Erin L. +4 more
openaire +3 more sources
Catalytic polymeric nanoreactors : more than a solid supported catalyst [PDF]
, 2012 Polymeric nanostructures can be synthesized where the catalytic motif is covalently attached within the core domain and protected from the environment by a polymeric shell.
Cotanda, Pepa +3 more
core +1 more source