Introduction:
The
Department was founded in 1987. Interest in structure, function and
inhibition of avian and mammalian retroviral proteases, the HIV protease
namely, permitted an early involvement in the rational design of anti-AIDS
drugs. Instrumental for this has been the capacity to supply the
required recombinant proteins in quality and quantity suitable for x-ray
structural studies.
The protein crystallography proper has been carried out at the
Department since late nineties with a new home diffraction
station. The
"flag projects" include elucidation of structural basis of non-active-site
inhibition of the HIV protease by monoclonal antibodies directed to the
enzyme flap and subunit dimerization regions as well as elucidation of
structural basis of subtleties of the HIV protease drug resistance.
Protein crystallography studies have further diversified also to solving
structures of other proteins of pathogenic importance.
Last but not least, the Department is involved in certain more "mundane"
projects, e.g. development of production protocols for recombinant-protein
antigens or recombinant forms of antibodies intended for clinical use.
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