Structural features of the interfaces in enzyme-inhibitor complexes.
Specific protein-protein interaction is essential for the function of life systems. A variety of computational methods are being extensively used now-a-days to investigate this interaction and to identify structural features of binding sites. In this paper, the informational structure analysis method was applied to the study of protein-protein interaction interfaces in enzyme-inhibitor complexes. The analysis of amino acid sequence by informational structure analysis method reveals three types of sites (ADD+, NORMAL and ADD-) which differ in the density of first rank elements in the informational structure. ADD+, NORMAL and ADD- sites also differ in their ability towards adaptive conformational reorganization which contributes to the formation of protein-protein interaction interfaces in enzyme-inhibitor complexes. The study of hydrolytic enzymes in complex with their protein inhibitors shows that at least one of the interaction interface sites is of ADD- type. ADD- sites possess an increased ability towards adaptive conformational changes thus enabling effective protein interaction.
Nekrasov
A N
AN
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences ul. Miklukho-Maklaya, 16/10, Moscow, 117997 Russia. alexei_nekrasov@mail.ru
Zinchenko
A A
AA
D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D025941:Protein Interaction Mapping / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*
D004791:Enzyme Inhibitors; D004798:Enzymes