Modificētās L-ornitīna δ-aminotransferāzes strukturālie pētījumi jaunu diazonamīda A struktūranalogu dizainam
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Latvijas Universitāte
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Abstract
Darba mērķi ir izstrādāt metodi rekombinantas modificētās ornitīna δ-aminotransferāzes (MOAT) produkcijai un kristalizēšanai, analizēt MOAT strukturālās atšķirības no ornitīna δ-aminotransferāzes (OAT), kā arī noteikt MOAT kristālu struktūru kompleksā ar Latvijas Organiskās sintēzes institūta pētnieku sintezētajiem diazonamīda A struktūranalogiem. Tādejādi, varētu noteikt MOAT un diazonamīda A struktūranalogu ķīmisko mijiedarbību veidu, iegūstot zināšanas jaunu MOAT inhibitoru dizainam.
Bakalaura darba laikā tika iegūts rekombinants, E.coli producēts, MOAT, kā arī MOAT kristālstruktūra kompleksā ar piridoksāla 5´ fosfātu.
Bakalaura darbs tika izstrādāts Latvijas Biomedicīnas pētījumu un studiju centrā, proteīnu kristalogrāfijas laboratorijā, Dr. biol. Kaspara Tāra vadībā.
The purpose of this work was to develop method for production and crystalization of recombinat modified ornithine δ-aminotransferase (MOAT), to analyse MOAT structural differences compared to ornithine δ-aminotransferase (OAT), and to obtain crystal structure of MOAT in complex with structural analogues of diazonamide A, sythesized by researchers from Latvian Institute of Organic Synthesis. In this way, one could determine chemical interaction’s between MOAT and structural analogues of diazonamide A, obtaining new knowledge for rational design of new MOAT inhibitors. During development of bachelors paper, production of recombinat, in E.coli produced MOAT was carried out and crystal structure of MOAT in complex with piridoxal 5’ phosphate was solved. This bachelors paper was developed in Latvian Biomedical Reasearch and Study Centere, in the laboratory of protein crystallography under supervision of Dr. Biol Kaspars Tārs.
The purpose of this work was to develop method for production and crystalization of recombinat modified ornithine δ-aminotransferase (MOAT), to analyse MOAT structural differences compared to ornithine δ-aminotransferase (OAT), and to obtain crystal structure of MOAT in complex with structural analogues of diazonamide A, sythesized by researchers from Latvian Institute of Organic Synthesis. In this way, one could determine chemical interaction’s between MOAT and structural analogues of diazonamide A, obtaining new knowledge for rational design of new MOAT inhibitors. During development of bachelors paper, production of recombinat, in E.coli produced MOAT was carried out and crystal structure of MOAT in complex with piridoxal 5’ phosphate was solved. This bachelors paper was developed in Latvian Biomedical Reasearch and Study Centere, in the laboratory of protein crystallography under supervision of Dr. Biol Kaspars Tārs.