Table of Contents
Sergey V. Verevka and Tatiana V. Grinenko
National Academy of Medical Sciences of Ukraine
Series: Protein Biochemistry, Synthesis, Structure and Cellular Functions
The ability to recognize functional partners is a base for interactions between proteins. These interactions can regulate multiple biological processes. However, when a binding site is not in accordance to the site, which has to be bound, there is no effective interaction between functional partners, so the regulation of the processes mediated by these partners is disturbed. If instead of high affinity sites on the protein surface their structural analogs are formed, the consequences for functional interactions can be even worse.
The appearance of such groups allows protein molecule efficiently take part into alien interactions disrupting natural regulation process. Pseudo-functional interactions of plasminogen can be considered as an example of these disruptions. It has been noticed the formation of the disordered structures, which are complementary to its binding sites. These structures differ by both appearance and gravity of consequences. Pathologic consequences of non-functional formation of high-affinity sites toward this protein are remarkable for their diversity, gravity and are the subject for special consideration. (Imprint: Nova)