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SSIPe is a method to calculate binding affinity changes (ΔΔGbind) of protein-protein interactions (PPIs) upon mutations at protein-protein interface. Starting from a PPI complex structure, SSPIe first generates multple structure and sequence alignments from PDB and STRING databases separately. The structural and sequence profiles are then combined with the physical energy function EvoEF to predict the impact of the mutations on PPI binding free energies. When a mutation does not take place at the interface, only the EvoEF force field will be used to predict the binding affinity change. SSIPe can be used to guide the designing and engineering of protein-protein interactions with enhanced binding affinity, and/or for understanding the roles of disease-related mutations associated with protein-protein interactions. The SSIPe server is developed to handel the cases where a mutation is only involved in a dimer. If users want to calculate the binding affinity change caused by a mutation in a multimer (multi-chain) protein, they can use the 'ComputeBinding' module of the EvoEF program coupling with the 'split' option. (>> Read more about SSIPe).

Please direct questions and inquiries to our Service System Discussion Board or contact Dr. Xiaoqiang Huang.

From May. 10 to Jul. 30, 2020 (CASP14 season), the SSIPe server will be closed to external users. Please use the standalone package during this period. Jobs already submitted will not be affected. We apologize for any inconvenience this may cause.

SSIPe Online Server (Example output)


Download SSIPe and Benchmark Datasets



Reference:

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