Search results for "Enzyme Catalysis and Regulation"

showing 1 items of 1 documents

Strong Cooperativity and Loose Geometry between CUB Domains Are the Basis for Procollagen C-Proteinase Enhancer Activity

2009

Procollagen C-proteinase enhancers (PCPE-1 and -2) specifically activate bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family during C-terminal processing of fibrillar collagen precursors. PCPEs consist of two CUB domains (CUB1 and CUB2) and one NTR domain separated by one short and one long linker. It was previously shown that PCPEs can strongly interact with procollagen molecules, but the exact mechanism by which they enhance BMP-1 activity remains largely unknown. Here, we used a series of deletion mutants of PCPE-1 and two chimeric constructs with repetitions of the same CUB domain to study the role of each domain and linker. Out of all the forms teste…

CooperativityPlasma protein bindingTransfectionBinding CompetitiveBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1Cell LineHumansAmino Acid SequenceBinding siteEnhancerMolecular BiologyGlycoproteinsExtracellular Matrix ProteinsBinding SitesEnzyme Catalysis and RegulationChemistryCircular DichroismCell BiologyCUB domainKineticsProcollagen peptidaseBiochemistryMutationBiophysicsElectrophoresis Polyacrylamide GelLinkerProcollagenProtein BindingJournal of Biological Chemistry
researchProduct