Proteins commonly form quaternary complexes to perform their biological functions. The main computational method used to predict these complexes is molecular docking which is mostly limited to predicting dimers. Here we introduce a new docking protocol, Distance Restraints- and Cyclic Symmetry-Imposed Packing (DR-SIP), which can predict the quaternary structures of homo-oligomeric transmembrane proteins (HoTPs) of any size (dimers or larger) without prior-knowledge of its native size. DR-SIP is able to recover 52.6% and 76.3% of HoTPs within the top-20 poses when given/not-given the complexes’ native size, respectively. Predictions can be further improved by making use of distance-based experimental data such as those from single-molecule FRET (smFRET).第58回 日本生物物理学会年
