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National Repository of Grey Literature 2 records found  Search took 0.00 seconds. 
Struktura a funkce rekombinantního P2X4 receptoru
 Rokič, Miloš ; Zemková, Hana (advisor) ; Vlachová, Viktorie (referee) ; Bendová, Zdeňka (referee)
4 Abstract Purinergic P2X receptors are membrane ion channels activated by extracellular ATP. There are seven isoforms of mammalian P2X receptors designated as P2X1-7, which according to their structure represent a specific family of ligand gated ionic channels, with extraordinary structural/functional properties. The P2X receptor consists of three subunits and each subunit has two transmembrane domains. Crystalographic data demonstrate that ionic channel pore is situated between the second transmembrane domains. Crystal structure of P2X4 receptor from the zebrafish (Danio rerio) is available in both open and closed state of the channel and the exact structure of ATP binding site is solved. The aim of this thesis was to study the structure-function relationships in a model of recombinant P2X4 receptor of the rat. By employing the point mutagenesis and electrophysiological recording, the functional importance of conserved cysteine residues in the ectodomain and amino acid residues which form the extracellular vestibule was investigated. All ten cysteins were substituted one by one with alanine or threonine and ATP-induced currents were measured from HEK293T cells expressing wild type (WT) and mutated P2X4 receptors. The results indicate that C116A, C126A, C149A and C165A mutations disrupt two disulfide bonds...
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Expression and characterization of recombinant capsid protein from HIV and its mutants: towards inhibition of virus assembly
 Sivá, Monika ; Konvalinka, Jan (advisor) ; Maloy Řezáčová, Pavlína (referee)
Human immunodeficiency virus infection has been a threat to the world for the last thirty years. It causes a condition called acquired immunodeficiency syndrome leading to complete collapse of immune system and death if not treated. There are many anti-HIV drugs that are part of the combined antiretroviral treatment but they only slow down the progress of the infection. Although the success of all the 31 antiviral agents is remarkable, the cure is not efficient enough. The research of potencial new HIV drugs is now focusing on new targets of viral inhibition. The capsid protein is a potential target of virion assembly and maturation inhibitors due to its multimerization features. The N-terminal domains of six capsid proteins create hexamers. These are connected to each other by dimers of the C-terminal domains according to X-ray and NMR studies. There are inhibitors that bind to the C-terminal domain, alter its conformation and weaken the protein-protein interaction of the dimer. Protein calorimetry is a method that could detect and quantify protein-protein interactions and thus capsid protein dimerization and its inhibition. We expressed and purified recombinant wild-type capsid protein and its C-terminal domain that both dimerize in solution and crystals. Their dimerization constant was determined by...
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