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Preliminary Crystallographic Study of ç-D-Crystalline Obtained from Patient`s Eye
Brynda, Jiří ; Řezáčová, Pavlína ; Štouračová, Renata ; Ondráček, Jan ; Kmoch, B. ; Asfaw, B. ; Elleder, M. ; Bezouška, K. ; Filipec, M. ; Sedláček, Juraj
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Anti-HIV Proteinase Monoclonal Antibody F11.2.32 That Inhibits Enzyme Activity
Štouračová, Renata ; Lescar, J. ; Brynda, Jiří ; RIottot, M. ; Chitarra, V. ; Fábry, Milan ; Hořejší, Magdalena ; Řezáčová, Pavlína ; Bentley, G. ; Sedláček, Juraj
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Vazba fenylnorstatinového inhibitoru na proteázu HIV-1: geometrie, protonace a interakce kapes podřadných míst analyzované při atomovém rozlišení
Brynda, Jiří ; Řezáčová, Pavlína ; Fábry, Milan ; Hořejší, Magdalena ; Štouračová, Renata ; Sedláček, Juraj ; Souček, Milan ; Hradilek, Martin ; Lepšík, Martin ; Konvalinka, Jan
The x-ray structure of a complex of HIV-1 protease (PR) with a phenylnorstatine inhibitor Z-Pns-Phe-Glu-Glu-NH2 has been determined at 1.03 A, the highest resolution so far reported for any HIV PR complex. The inhibiot shows subnanomolar Ki values for both the wild-type PR and the variant representing one of the most common mutations linked to resistance development. The structure displays a unique pattern of hydrogen bonding to the two catalytic aspartate residues. The high resolution permints to assess the donor/acceptor relations of this hydrogen bonding and to indicate a proton shared by the two catalytic residues. Structural mechanism for the unimpaired inhibition of the protease Val82Ala mutant is also suggested, based on energy calculations and analyses
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Charakterizace klonů odvozených od kolorektální nádorově buněčné linie HT29
Šloncová, Eva ; Kučerová, Dana ; Vojtěchová, Martina ; Turečková, Jolana ; Tuháčková, Zdena ; Sovová, Vlasta
During our analysis of HT29 cell line we established several clones, which differed in the expression of some molecular markers, e.g. phosphorylation of Src protein, PKCbeta2 activity, CEA-CAM1 expression and in the response to the differentiating effect of sodium butyrate, indicated by activity of alkaline phosphatase
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Interaction of sperm surface proteins in the reproduction process
Jonáková, Věra ; Kraus, Marek ; Maňásková, Pavla ; Liberda, J. ; Tichá, M.
Mammalian fertilization includes highly regulated biochemical interactions between complementary molecules located on the surfaces of both gametes as well as those present in the natural environment of the gametes. Boar seminal plasma proteins AQN, AWN spermadhesins and DQH protein that are bound to the sperm at ejaculation play important role in the reproduction process. Binding of sperm to epithelial cells, recognition of gametes and binding of sperm to glycoprotein of zona pellucida are mediated by protein-saccharide interaction, lektin-type interaction. Another type of interaction (protein-protein) participates in the formation of aggregated forms, which seem to be the natural functional forms of seminal plasma proteins. Protein aggregates form the sperm coating layers and their re-modeling in the female reproductive tract is imporatnt for the sperm capacitation and for the primary binding of spermto the ovum.
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