SISYPHUS database of protein structure alignments

SISYPHUS database of protein structure alignments provides structural alignments of proteins to analyze alternative folds, context-dependent conformations, oligomerisation, and gene-duplication–related structural changes for studies of protein evolution.

Key Features:

• Handling Alternative Folds: Aligns proteins exhibiting alternative folds and multiple conformational states to capture non-trivial evolutionary relationships.
• Context-Dependent Conformations: Identifies and aligns variable regions that adopt different conformations depending on their context, enabling analysis of flexible regions and oligomeric interface formation.
• Oligomerisation Analysis: Examines oligomerisation to elucidate how oligomer formation contributes to fold evolution.
• Gene Duplication Insights: Analyzes impacts of gene duplication, including asymmetry in homo-oligomeric structures and subsequent architectural modifications.

Scientific Applications:

• Evolutionary Biology: Investigating how alternative folds and oligomerisation contribute to the diversification of protein functions.
• Structural Genomics: Understanding the relationship between gene duplication events and structural changes in proteins.
• Functional Analysis: Exploring context-dependent conformational changes that underlie functional adaptations in proteins.

Methodology:

Uses advanced algorithms to perform protein structure alignments that account for conserved and variable regions and integrates data on oligomerisation and gene duplication effects.