The subject of this thesis was to structurally characterize three groups of proteins.
Nicastrin (a subunit of the γ-secretase) was examined with the aim to gain insight into its structure and to open the possibilities of screening for active compounds that could block production of the B-amyloid (Alzheimer disease causative agent) by γ-secretase.
Structural studies on cyanobacterial biliprotein lyases from Mastigocladus laminosus, Synechococcus sp. PCC7002, and Nostoc sp. PCC7120 were meant to reveal the mechanism of chromophore attachment.
Three structures of integrases from Enterobacteriaceae genomic islands were obtained: arm-type binding domain of HPI (from Yersinia pestis) and HAI7 (from Erwinia carovotora) integrases along with HPI integrase complex with its attachment site on the DNA. Due to differences in ternary structure, these integrases can be classified as a novel type of fold. The structure of integrase complex with DNA gives insight into the base recognition mode. A dimerization interface, which can play role in the functionality of the whole HPI integrase, was also determined.
«
The subject of this thesis was to structurally characterize three groups of proteins.
Nicastrin (a subunit of the γ-secretase) was examined with the aim to gain insight into its structure and to open the possibilities of screening for active compounds that could block production of the B-amyloid (Alzheimer disease causative agent) by γ-secretase.
Structural studies on cyanobacterial biliprotein lyases from Mastigocladus laminosus, Synechococcus sp. PCC7002, and Nostoc sp. PCC7120 were mea...
»