The Institute of Enzymology

Research groups

Maria Vas

Group leader: Dr. Maria Vas

Modular organisation of protein structure into domains or subunits is a general feature of the most enzyme molecules. Enzymes are proteins which execute and controll all functions in living organisms. Modules are important in various structural and functional aspects. First, their independent or cooperative contribution to formation of the native protein fold is an important question and one of our aims is the clarification of such mechanisms. Second, relative movement of larger structural units, modules or domains within a protein molecule, the most spectacular representatives of conformational flexibility, are essential for enzyme function. By the aid of enzymological and biophysical in vitro methodology we are dealing with establishing the structural principles that govern such movements and the mechanism of communication between modules.

Role of Modular Organisation in Folding and Function of Proteins

The research project, on the one hand, is dealing with the mechanism of native structure formation of multidomain and oligomeric proteins; i.e. with the question, whether the domains and subunits are independent folding units or fold co-operatively into the native conformation. On the other hand, our aim is to establish the role of domain-domain communication in the biological function of proteins and delineate, in structural terms, its mechanism.

Enzymatic activation of antiviral prodrugs: phosphorylation by 3-phosphoglycerate kinase

An important group of the chemicals with antiviral effect includes various nucleosides, among them compounds with unnatural L-configuration. Upon entry into the cell, the nucleoside prodrug must be phosphorylated by a cascade of cellular kinases to the pharmacologically active triphosphate. We plan to understand the structural basis of enzymatic phosphorylation of various nucleoside diphosphates and convert this knowledge into designing new effective drugs against HIV.