CCProf: exploring conformational change profile of proteins

Area of Science:

• Biochemistry
• Structural Biology
• Bioinformatics

Background:

• Proteins undergo critical conformational changes upon molecular interactions (ligands, ions, other proteins).
• Understanding these dynamic structural shifts is key to elucidating protein function and biological processes.

Purpose of the Study:

• Introduce the CCProf platform for studying protein conformational changes.
• Provide an integrated view of multiple biological features to explore causes of conformational changes.
• Facilitate visual analysis of protein dynamics and interactions.

Main Methods:

• Developed the CCProf platform integrating 10 biological features.
• Compiled a dataset of 986,187 protein structure pairs for 3123 proteins.
• Implemented a 3D visualization tool for pre- and post-change structures and binding targets.

Main Results:

• CCProf offers a comprehensive, visually aligned view of protein conformational changes and associated features.
• The platform includes data on conformational change profiles (CCP), binding sites, secondary structures, conservation, and more.
• A large dataset and 3D visualization tools are available for detailed analysis.

Conclusions:

• CCProf serves as a valuable resource for researchers investigating protein dynamics and molecular interactions.
• The integrated data and visualization capabilities facilitate the discovery of novel insights into protein conformational changes.
• All data and intermediate results are downloadable for further research and analysis.