Burcu Aykaç Fas

MAVISp provides a modular structural framework for analyzing protein variant effects, offering over eight million variants across 1000 proteins with curated data and a web server for accessibility.

The paper models the structure of the active NOX2 complex using AlphaFold2 and experimental data, revealing the role of disordered regions in subunit assembly.

The paper evaluates 43 methods for predicting intrinsically disordered regions and binding regions in proteins, finding that deep learning methods outperform older physicochemical approaches but binding prediction remains challenging.