Motivation: A wide range of fundamental biological processes are mediated by membrane proteins. Despite their large number and importance, less than 1% of all 3D protein structures deposited in the Protein Data Bank are of membrane proteins. This is mainly due to the challenges of crystallizing such proteins or performing NMR spectroscopy analyses. All the more so, there is only a small number of membrane protein-protein complexes with known structure. Therefore, developing computational tools for docking membrane proteins is crucial. Numerous methods for docking globular proteins exist, however few have been developed especially for membrane proteins and designed to address docking within the lipid bilayer environment. Results: We present a novel algorithm, Memdock, for docking α-helical membrane proteins which takes into consideration the lipid bilayer environment for docking as well as for refining and ranking the docking candidates. We show that our algorithm improves both the docking accuracy and the candidates ranking compared to a standard protein-protein docking algorithm.
Bibliographical noteFunding Information:
This research was supported by the Israel Science Foundation (Grant No. 1112/12), the I-CORE program of the Budgeting and Planning Committee and the Israel Science Foundation (center No. 1775/12) and by the Hermann Minkowski Minerva Geometry Center. N.H. acknowledges the Edmond J.Safra Bioinformatics Center fellowship.
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