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 metho...
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Published in | Journal of biomolecular structure & dynamics Vol. 28; no. 1; pp. 85 - 96 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
England
Taylor & Francis Group
01.08.2010
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0739-1102 1538-0254 |
DOI: | 10.1080/07391102.2010.10507345 |