ArticleStructure (London, England : 1993)2021
PDB-wide identification of physiological hetero-oligomeric assemblies based on conserved quaternary structure geometry.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Reciprocal best matching: a new pipeline for scoring models with unknown stoichiometry in CASP experiments.BMC bioinformatics · 2026Article
- QSProteome: a community-driven interactive platform for large-scale exploration and evaluation of predicted protein complex structures.Nucleic acids research · 2026Article
- A suite of designed protein cages using machine learning and protein fragment-based protocols.Structure (London, England : 1993) · 2024Article
- A Suite of Designed Protein Cages Using Machine Learning Algorithms and Protein Fragment-Based Protocols.bioRxiv : the preprint server for biology · 2023Article
- Protein complexes in cells by AI-assisted structural proteomics.Molecular systems biology · 2023Article
- Greater than the sum of parts: Mechanisms of metabolic regulation by enzyme filaments.Current opinion in structural biology · 2023Review
- The protein common assembly database (ProtCAD)-a comprehensive structural resource of protein complexes.Nucleic acids research · 2023Article
- QSalignWeb: A Server to Predict and Analyze Protein Quaternary Structure.Frontiers in molecular biosciences · 2021Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An accurate understanding of biomolecular mechanisms and diseases requires information on protein quaternary structure (QS). A critical challenge in inferring QS information from crystallography data is distinguishing biological interfaces from fortuitous crystal-packing contacts. Here, we employ QS conservation across homologs to infer the biological relevance of hetero-oligomers. We compare the structures and compositions of hetero-oligomers, which allow us to annotate 7,810 complexes as physiologically relevant, 1,060 as likely errors, and 1,432 with comparative information on subunit stoichiometry and composition. Excluding immunoglobulins, these annotations encompass over 51% of hetero-oligomers in the PDB. We curate a dataset of 577 hetero-oligomeric complexes to benchmark these annotations, which reveals an accuracy >94%. When homology information is not available, we compare QS across repositories (PDB, PISA, and EPPIC) to derive confidence estimates. This work provides high-quality annotations along with a large benchmark dataset of hetero-assemblies.
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