Source:IWBBIO 2014 (2nd International Work-Conference on Bioinformatics and Biomedical Engineering), Granada, Spain, 2014
Most of the current docking procedures are focused on fine conformational adjustment of assembled complexes and fail to reproduce large-scale motions. Our approach based on the coarse-grained modeling of flexible macromolecules overcomes these limitations. CABSDock procedure used in this work employs coarse-grained model CABS – efficient and versatile tool for modeling of proteins structure, dynamics and interactions [1-4].
In this work CABSDock was used to model assembly process of troponin C(TnC) with the N-terminal helix of the troponin I(TnI). TnC/TnI binding was investigated for both cardiac and skeletal troponin. TnI fragment was modeled allowing its unbiased movement. Entire structure of TnC domain was also treated as fully flexible, although its motion was restricted to near-native conformations. Binding of the TnI fragment changed the orientation between both domains. This picture provides valuable insight into mechanistic description of troponin function.