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Computed structures of core eukaryotic protein complexes.
- Source :
-
Science (New York, N.Y.) [Science] 2021 Dec 10; Vol. 374 (6573), pp. eabm4805. Date of Electronic Publication: 2021 Dec 10. - Publication Year :
- 2021
-
Abstract
- Protein-protein interactions play critical roles in biology, but the structures of many eukaryotic protein complexes are unknown, and there are likely many interactions not yet identified. We take advantage of advances in proteome-wide amino acid coevolution analysis and deep-learning–based structure modeling to systematically identify and build accurate models of core eukaryotic protein complexes within the Saccharomyces cerevisiae proteome. We use a combination of RoseTTAFold and AlphaFold to screen through paired multiple sequence alignments for 8.3 million pairs of yeast proteins, identify 1505 likely to interact, and build structure models for 106 previously unidentified assemblies and 806 that have not been structurally characterized. These complexes, which have as many as five subunits, play roles in almost all key processes in eukaryotic cells and provide broad insights into biological function.
- Subjects :
- Acyltransferases chemistry
Acyltransferases metabolism
Chromosome Segregation
Computational Biology
Computer Simulation
DNA Repair
Evolution, Molecular
Homologous Recombination
Ligases chemistry
Ligases metabolism
Membrane Proteins chemistry
Membrane Proteins metabolism
Models, Molecular
Protein Biosynthesis
Protein Conformation
Protein Interaction Maps
Proteome metabolism
Ribosomes metabolism
Saccharomyces cerevisiae chemistry
Ubiquitin chemistry
Ubiquitin metabolism
Deep Learning
Multiprotein Complexes chemistry
Multiprotein Complexes metabolism
Protein Interaction Mapping
Proteome chemistry
Saccharomyces cerevisiae Proteins chemistry
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 374
- Issue :
- 6573
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 34762488
- Full Text :
- https://doi.org/10.1126/science.abm4805