期刊
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
卷 28, 期 1, 页码 85-96出版社
ADENINE PRESS
DOI: 10.1080/07391102.2010.10507345
关键词
Informational structure of proteins; Enzyme-inhibitor complex; Protein-protein interaction
资金
- Russian Federation [NSh-5207.2010.4]
- Russian Academy of Sciences
Specilic 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.
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