Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 89, Issue 12, Pages 1647-1672Publisher
WILEY
DOI: 10.1002/prot.26247
Keywords
CASP; community-wide experiment; cryo-EM; protein structure prediction; X-ray crystallography
Categories
Funding
- ANID Becas Chile studentship [72180329]
- Cancer Prevention and Research Institute of Texas [RP180813]
- Deutsche Forschungsgemeinschaft [Bo1150/17-1]
- National Institute of General Medical Sciences [GM100482]
- National Institutes of Health [1R01GM137021, GM117373, P01-CA092584, P41-GM103311, P41-GM103832, R01-AI102546, R01-GM079429, R35-CA220430, R37-AI20459, S10-OD021600]
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek [714.014.002]
- Wellcome Trust [106077/Z/14/Z]
- Italian Ministry of Health [RF2016-02364123]
- National Institute of Allergy and Infectious Diseases, National Institutes of Health [HHSN272201700060C]
- U.S. Department of Energy [DEAC02-06CH11357, DE-AC36-08GO28308]
- Office of Biological and Environmental Research in the DOE Office of Science
- Swiss Institute of Bioinformatics SIB
- Wellcome Trust [106077/Z/14/Z] Funding Source: Wellcome Trust
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The ability to predict protein structures in CASP14 has significantly improved, with many challenging targets modeled accurately. Experimentalists highlighted that computational models can accurately reproduce critical structural features and can guide further studies on biologically-relevant properties of proteins.
The biological and functional significance of selected Critical Assessment of Techniques for Protein Structure Prediction 14 (CASP14) targets are described by the authors of the structures. The authors highlight the most relevant features of the target proteins and discuss how well these features were reproduced in the respective submitted predictions. The overall ability to predict three-dimensional structures of proteins has improved remarkably in CASP14, and many difficult targets were modeled with impressive accuracy. For the first time in the history of CASP, the experimentalists not only highlighted that computational models can accurately reproduce the most critical structural features observed in their targets, but also envisaged that models could serve as a guidance for further studies of biologically-relevant properties of proteins.
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