Flexible docking of the fragment of the troponin I to the troponin C

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 ov ercomes t hese limitations. CA BSDock proc edure us ed in t his work employs c oarse-grained m odel CA BS – efficient and v ersatile t ool for modeling of proteins structure, dynamics and interactions [1-4]. In t his w ork CABSDock w as us ed t o model a ssembly proc ess of t roponin 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 i ts un biased m ovement. E ntire s tructure of TnC do main w as also treated as fully flexible, although i ts 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.