Published in

Wiley, Proteins: Structure, Function, and Bioinformatics, 12(91), p. 1658-1683, 2023

DOI: 10.1002/prot.26609

Links

Tools

Export citation

Search in Google Scholar

Impact of AlphaFold on structure prediction of protein complexes: The CASP15‐CAPRI experiment

Journal article published in 2023 by Marc F. Lensink ORCID, Guillaume Brysbaert, Nessim Raouraoua, Paul A. Bates ORCID, Marco Giulini, Rodrigo V. Honorato, Charlotte van Noort, Joao M. C. Teixeira ORCID, Alexandre M. J. J. Bonvin ORCID, Ren Kong, Hang Shi, Xufeng Lu, Shan Chang ORCID, Jian Liu, Zhiye Guo and other authors.
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

Full text: Unavailable

Green circle
Preprint: archiving allowed
Orange circle
Postprint: archiving restricted
Red circle
Published version: archiving forbidden
Data provided by SHERPA/RoMEO

Abstract

AbstractWe present the results for CAPRI Round 54, the 5th joint CASP‐CAPRI protein assembly prediction challenge. The Round offered 37 targets, including 14 homodimers, 3 homo‐trimers, 13 heterodimers including 3 antibody–antigen complexes, and 7 large assemblies. On average ~70 CASP and CAPRI predictor groups, including more than 20 automatics servers, submitted models for each target. A total of 21 941 models submitted by these groups and by 15 CAPRI scorer groups were evaluated using the CAPRI model quality measures and the DockQ score consolidating these measures. The prediction performance was quantified by a weighted score based on the number of models of acceptable quality or higher submitted by each group among their five best models. Results show substantial progress achieved across a significant fraction of the 60+ participating groups. High‐quality models were produced for about 40% of the targets compared to 8% two years earlier. This remarkable improvement is due to the wide use of the AlphaFold2 and AlphaFold2‐Multimer software and the confidence metrics they provide. Notably, expanded sampling of candidate solutions by manipulating these deep learning inference engines, enriching multiple sequence alignments, or integration of advanced modeling tools, enabled top performing groups to exceed the performance of a standard AlphaFold2‐Multimer version used as a yard stick. This notwithstanding, performance remained poor for complexes with antibodies and nanobodies, where evolutionary relationships between the binding partners are lacking, and for complexes featuring conformational flexibility, clearly indicating that the prediction of protein complexes remains a challenging problem.