Significance of Knotted Structures for Function of Proteins and Nucleic Acids
Poster Session II
49 – POS
Board 21
Multiscale Flexible Docking of Troponin I to Troponin C
Jacek Wabik
, Mateusz Kurcinski, Andrzej Kolinski.
Warsaw University, Warsaw, Poland.
Most of the current protein-protein docking procedures fail to reproduce large-scale motions of a
modeled complex. Our approach based on the coarse-grained modeling of flexible proteins
overcomes this limitation. The CABSDock procedure used in this work employs a coarse-
grained CABS model, an efficient and versatile tool for modeling protein structure, dynamics
and interactions [1-4].
In this work CABSDock was used to model the assembly process of troponin C (TnC) with the
N-terminal helix of troponin I (TnI). TnC/TnI binding was investigated for both cardiac and
skeletal troponin. The TnI fragment was modeled as fully flexible protein chain, without any
restraints. The entire structure of the TnC was also treated as flexible, although each domain was
restricted to near-native conformation. Our simulations show that binding of TnI fragment
changes orientation between N-terminal and C-terminal domain of TnC. The obtained picture of
the binding process provides a valuable insight into the mechanistic description of troponin
function.
[1] S. Kmiecik, D. Gront, M. Kouza, A. Kolinski, J Phys. Chem. B., 2012, 116 (23), 7026–7032
[2] S. Kmiecik,A. Kolinski, Biophys. J., 2008, 94, 726-736
[3] J. Wabik, S. Kmiecik, D. Gront, M. Kouza, A. Koliński, Int. J. Mol. Sci.,2013, 14, 9893-9905
[4] A. Kolinski, J.M. Bujnicki, Proteins, 2005, 61, 84-90
- 94 -
