Structure/function analysis of complement protein C2

The complement system is a very important component of the innate immunodefence, which promotes and regulates the pagocytosis or lysis of foreign cells, particles or macromolecules and host tissue breakdown products. The system is composed of more than thirty proteins, both soluble and membranebound, that interact with each other, when the system is activated by various stimuli. Upon stimulation, a subcomponent of the membrane bound C1-complex activates the glycoprotein C4 by cleaving it into C4a and C4b. C4b bind s to the membrane of the complement activator and interacts with C2, which thereupon is cleaved into C2a and C2b complex, which is known as C3-convertase of the classical pathway of complement activation. To investigate the interactions between the human glycoprotein C2 and other proteins such as C4, C1s, C3 and DAF, several molecularbiological techniques are use. The project involves expression, in a bacterial or techniques are used. The project involves expression, in a bacterial or yeast system, of the domains of C2 and examination of their interaction with the mentioned proteins. Additionally, techniques for protein isolation will be used to purify recombinant C2 domains and to perform structural analysis.