MFIB

MFIB collects and classifies protein complexes wherein all constituent protein chains are intrinsically disordered in isolation but fold into well-defined 3D complex structures upon binding, a phenomenon termed cooperative folding and binding or mutual synergistic folding (MSF).

Key Features:

• Database curation: Annotates hundreds of protein complexes fulfilling MSF criteria with an evidence coverage label that allows inclusion of complexes of multi(sub)domain monomers with partial MSF.
• Structural clustering: Clusters complexes based on structural similarity and domain types.
• Evidence levels: Assigns different evidence levels to each entry to indicate confidence in the classification.

Scientific Applications:

• Intrinsically disordered protein research: Provides a specialized resource for studying protein complexes formed by mutual folding of intrinsically disordered protein chains upon binding.
• Structural classification: Enables analysis of relationships between MSF complexes through structural similarity and domain type clustering.

Methodology:

Complexes are collected and annotated based on criteria of mutual synergistic folding, with entries classified by evidence levels and clustered according to structural similarity and domain types.