The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain. [PDF]
, 2016 GPIHBP1 is a glycolipid-anchored membrane protein of capillary endothelial cells that binds lipoprotein lipase (LPL) within the interstitial space and shuttles it to the capillary lumen.
Beigneux, Anne P +9 more
core +4 more sources
Complete Determination of the Pin1 Catalytic Domain Thermodynamic Cycle by NMR Lineshape Analysis [PDF]
, 2011 The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers.
De, Soumya +5 more
core +2 more sources
Zinc Binding Catalytic Domain of Human Tankyrase 1 [PDF]
Journal of Molecular Biology, 2008 Tankyrases are recently discovered proteins implicated in many important functions in the cell including telomere homeostasis and mitosis. Tankyrase modulates the activity of target proteins through poly(ADP-ribosyl)ation, and here we report the structure of the catalytic poly(ADP-ribose) polymerase (PARP) domain of human tankyrase 1. This is the first
Lari, Lehtiö +9 more
openaire +2 more sources
Modulation of catalytic activity in multi-domain protein tyrosine phosphatases. [PDF]
PLoS ONE, 2011 Signaling mechanisms involving protein tyrosine phosphatases govern several cellular and developmental processes. These enzymes are regulated by several mechanisms which include variation in the catalytic turnover rate based on redox stimuli, subcellular
Lalima L Madan +5 more
doaj +1 more source
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.
Bosman, Liu, Wang, Yan
core +2 more sources
The Dimerization Domain in DapE Enzymes Is Required for Catalysis [PDF]
, 2013 The emergence of antibiotic-resistant bacterial strains underscores the importance of identifying new drug targets and developing new antimicrobial compounds.
Gutierrez, Blanca +9 more
core +8 more sources
Catalytic Domain Architecture of Metzincin Metalloproteases [PDF]
Journal of Biological Chemistry, 2009 Metalloproteases cleave proteins and peptides, and deregulation of their function leads to pathology. An understanding of their structure and mechanisms of action is necessary to the development of strategies for their regulation. Among metallopeptidases are the metzincins, which are mostly multidomain proteins with approximately 130-260-residue ...
openaire +2 more sources
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
Controlling tetramer formation, subunit rotation and DNA ligation during Hin-catalyzed DNA inversion. [PDF]
, 2015 Two critical steps controlling serine recombinase activity are the remodeling of dimers into the chemically active synaptic tetramer and the regulation of subunit rotation during DNA exchange.
Chang, Yong, Johnson, Reid C
core +3 more sources
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