Zepyros: A webserver to evaluate the shape complementarity of protein-protein interfaces

Abstract

Shape complementarity of molecular surfaces at the interfaces is a well-known characteristic of protein-protein binding regions, and it is critical in influencing the stability of the complex. Measuring such complementarity is at the basis of methods for both the prediction of possible interactions and for the design/optimization of speficic ones. However, only a limited number of tools are currently available to efficiently and rapidly assess it. Here, we introduce Zepyros, a webserver for fast measuring of the shape complementarity between two molecular interfaces of a given protein-protein complex using structural information. Zepyros is implemented as a publicly available tool with a user-friendly interface. Our server can be found at the following link (all major browser supported): https://zepyros.bio-groups.com

4 pages, 1 figure

References in corpus (4)

• Investigating the side-chain structural organization behind the stability of protein folding and binding
• Protein folding and binding can emerge as evolutionary spandrels through structural coupling
• Electrostatic complementarity at the interface drives transient protein-protein interactions
• Shape Complementarity Optimization of Antibody-Antigen Interfaces: the Application to SARS-CoV-2 Spike Protein