Discriminating physiological from non-physiological interfaces in structures of protein complexes: A community-wide study.

ABSTRACT: Reliably scoring and ranking candidate models of protein complexes and assigning their oligomeric state from the structure of the crystal lattice represent outstanding challenges. A community-wide effort was launched to tackle these challenges. The latest resources on protein complexes and interfaces were exploited to derive a benchmark dataset consisting of 1677 homodimer protein crystal structures, including a balanced mix of physiological and non-physiological complexes. The non-physiological complexes in the benchmark were selected to bury a similar or larger interface area than their physiological counterparts, making it more difficult for scoring functions to differentiate between them. Next, 252 functions for scoring protein-protein interfaces previously developed by 13 groups were

SUBMITTER: Schweke H 

PROVIDER: S-EPMC10937251 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature