ComSin

ComSin provides a curated database of 24,910 protein structure pairs derived from the Protein Data Bank (PDB) that represent bound (complex) and unbound (single) states to support analysis of structural transitions associated with complex formation.

Key Features:

• Extensive dataset: Contains 24,910 protein structure pairs, including 2,448 identical proteins and 7,129 pairs with ≥90% sequence identity, covering bound and unbound states.
• Intrinsic disorder analysis: Identifies regions of intrinsic disorder and documents disorder-to-order and order-to-disorder transitions upon complex formation.
• Sequence similarity search: Enables comparison of sequence identity between bound and unbound forms to assess homologous relationships and conservation.
• Interaction interface validation: Annotates and validates interaction interfaces of protein complexes to support analyses of binding and complex stability.
• Structural transition studies: Provides data and annotations for analyzing conformational changes associated with complex formation.
• Comparative structural analysis: Supports detailed comparisons of structural differences between proteins in bound and unbound states.

Scientific Applications:

• Protein–protein interaction studies: Enables investigation of how binding alters structure and interaction interfaces in protein complexes.
• Structural biology and conformational analysis: Supports analysis of disorder-to-order and order-to-disorder transitions and conformational rearrangements.
• Molecular dynamics and modeling: Provides benchmark pairs for modeling conformational changes and validating simulation results.
• Therapeutic targeting and drug discovery: Supplies structural and interface information relevant to targeting protein complexes and designing modulators.

Methodology:

Protein structure pairs were selected from the complete PDB by identifying entries that represent the same protein in bound (complex) and unbound (single) states, with inclusion of identical proteins and highly similar homologs to capture significant structural transitions upon complex formation.