IBIS

IBIS predicts and annotates protein interaction partners and binding sites, including proteins, chemicals, nucleic acids, and peptides, to map biomolecular interaction networks for structural and functional analysis.

Key Features:

• Experimental complex reporting: Reports experimentally determined structural complexes involving the queried protein.
• Homology-based inference: Infers interactions by examining protein complexes formed with homologous proteins.
• Binding partner annotation: Provides comprehensive annotations for binding partners including proteins, chemicals, nucleic acids, and peptides.
• Binding-site clustering: Clusters similar binding sites by leveraging conserved sequences and structures.
• Interaction verification algorithms: Verifies inferred interactions using criteria such as evolutionary conservation, biological significance of binding partners, interface size and stability, and corroborative literature evidence.
• Interaction network mapping: Maps extensive biomolecular interaction networks for query proteins.

Scientific Applications:

• Structural biology: Identify and analyze protein binding sites and interaction interfaces from structural complexes and homolog-derived inferences.
• Molecular biology: Predict interacting partners to guide functional characterization of proteins and their roles in biological processes.
• Bioinformatics: Integrate sequence and structural conservation to annotate interaction networks and support computational studies of protein interactions.

Methodology:

IBIS reports experimentally determined complexes and examines complexes of homologous proteins to infer interactions, clusters binding sites based on sequence and structural conservation, and applies algorithms that verify inferred interactions using evolutionary conservation, biological significance of binding partners, interface size and stability, and corroborative literature evidence.