MAPPIS

MAPPIS aligns protein-protein interfaces to identify spatially conserved physico-chemical interactions across sets of protein-protein complexes.

Key Features:

• Multiple Alignment of PPIs: Performs multiple alignment of protein-protein interfaces to compare the spatial arrangement of interactions across different complexes, independent of sequence or fold similarity.
• Recognition of Conserved Physico-chemical Interactions: Identifies spatially conserved physico-chemical properties within interfaces, including energetically significant hot-spot residues.
• Comprehensive Interaction Output: Produces an exhaustive list of shared interaction properties across the input protein-protein complexes.

Scientific Applications:

• Predicting Binding Sites: Uses spatially conserved interaction patterns to predict potential binding sites on proteins relevant to drug design and therapeutic interventions.
• Functional Annotation: Infers protein function from shared interaction motifs observed across multiple complexes.
• Protein Engineering: Guides engineering of proteins by revealing interaction motifs and hot-spot residues that determine binding properties.

Methodology:

MAPPIS aligns multiple protein-protein interfaces to identify common physico-chemical interactions without relying on sequence or structural (fold) similarity; the input is a set of protein-protein complexes and the output is a list of conserved interaction properties.