Science (American Association for the Advancement of Science), 2021-12, Vol.374 (6573), p.eabm4805-eabm4805
- Humphreys, Ian R
- Pei, Jimin
- Baek, Minkyung
- Krishnakumar, Aditya
- Anishchenko, Ivan
- Ovchinnikov, Sergey
- Zhang, Jing
- Ness, Travis J
- Banjade, Sudeep
- Bagde, Saket R
- Stancheva, Viktoriya G
- Li, Xiao-Han
- Liu, Kaixian
- Zheng, Zhi
- Barrero, Daniel J
- Roy, Upasana
- Kuper, Jochen
- Fernández, Israel S
- Szakal, Barnabas
- Branzei, Dana
- Rizo, Josep
- Kisker, Caroline
- Greene, Eric C
- Biggins, Sue
- Keeney, Scott
- Miller, Elizabeth A
- Fromme, J Christopher
- Hendrickson, Tamara L
- Cong, Qian
- Baker, David
2021
Volltextzugriff (PDF)
Details
- Autor(en) / Beteiligte
- Humphreys, Ian R
- Pei, Jimin
- Baek, Minkyung
- Krishnakumar, Aditya
- Anishchenko, Ivan
- Ovchinnikov, Sergey
- Zhang, Jing
- Ness, Travis J
- Banjade, Sudeep
- Bagde, Saket R
- Stancheva, Viktoriya G
- Li, Xiao-Han
- Liu, Kaixian
- Zheng, Zhi
- Barrero, Daniel J
- Roy, Upasana
- Kuper, Jochen
- Fernández, Israel S
- Szakal, Barnabas
- Branzei, Dana
- Rizo, Josep
- Kisker, Caroline
- Greene, Eric C
- Biggins, Sue
- Keeney, Scott
- Miller, Elizabeth A
- Fromme, J Christopher
- Hendrickson, Tamara L
- Cong, Qian
- Baker, David
- Titel
- Computed structures of core eukaryotic protein complexes
- Ist Teil von
- Science (American Association for the Advancement of Science), 2021-12, Vol.374 (6573), p.eabm4805-eabm4805
- Ort / Verlag
- United States: The American Association for the Advancement of Science
- Erscheinungsjahr
- 2021
- Quelle
- American Association for the Advancement of Science
- Beschreibungen/Notizen
- 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 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0036-8075eISSN: 1095-9203DOI: 10.1126/science.abm4805Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7612107
- Format
- –
- Schlagworte
- Accuracy, Acyltransferases - chemistry, Acyltransferases - metabolism, Amino acid sequence, Amino acids, Anemia, Assemblies, Assembly, Biological activity, Biology, C-Terminus, Cancer, Chromosome Segregation, Coevolution, Computational Biology, Computer Simulation, Deep Learning, Deoxyribonucleic acid, DNA, DNA Repair, Eukaryotes, Evolution, Molecular, Experimental methods, Fanconi syndrome, Gene sequencing, Genomes, Glycosylphosphatidylinositol, Homologous Recombination, Homology, Ligases - chemistry, Ligases - metabolism, Mass spectrometry, Mass spectroscopy, Membrane Proteins - chemistry, Membrane Proteins - metabolism, Microprocessors, Models, Molecular, Multiprotein Complexes - chemistry, Multiprotein Complexes - metabolism, Mutation, Neurodevelopmental disorders, Prokaryotes, Protein Biosynthesis, Protein Conformation, Protein interaction, Protein Interaction Mapping, Protein Interaction Maps, Protein structure, Protein transport, Proteins, Proteome - chemistry, Proteome - metabolism, Proteomes, Repair, Research methodology, Ribosomes - metabolism, Roles, Saccharomyces cerevisiae, Saccharomyces cerevisiae - chemistry, Saccharomyces cerevisiae Proteins - chemistry, Saccharomyces cerevisiae Proteins - metabolism, Single-stranded DNA, Teaching methods, Transcription, Trimers, Ubiquitin - chemistry, Ubiquitin - metabolism, Yeast, Yeasts