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AFFIPred: AlphaFold2 Structure-based Functional Impact Prediction of Missense Variations
Open accessPreprint — published as 10.1002/pro.70030 · Paper page
Abstract
Structural information holds immense potential for pathogenicity prediction of missense variations, albeit structure-based pathogenicity classifiers are limited compared to their sequence-based counterparts due to the well-known gap between sequence and structure data. Leveraging the highly accurate protein structure prediction method, AlphaFold2 (AF2), we introduce AFFIPred, an ensemble machine learning classifier that combines established sequence and AF2-based structural characteristics to predict disease-causing missense variant pathogenicity. Based on the assessments on unseen datasets, AFFIPred reached a comparable level of performance with the state-of-the-art predictors such as AlphaMissense and Rhapsody. We also showed that the recruitment of AF2 structures that are full-length and represent the unbound states ensures more precise SASA calculations compared to the recruitment of experimental structures. Second, in line with the the completeness of the AF2 structures, their use provide a more comprehensive view of the structural characteristics of the missense variation datasets by capturing all variants. AFFIPred maintains high-level accuracy without the well-known limitations of structure-based pathogenicity classifiers, paving the way for the development of more sophisticated structure-based methods without PDB dependence. AFFIPred has predicted over 210 million variations of the human proteome, which are accessible at https://affipred.timucinlab.com/ .
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
A structural biology community assessment of AlphaFold2 applications
Akdel, M., Pires, D. E. V., Pardo, E. P., Jänes, J., Zalevsky, A. O., Mészáros, B., Bryant, P., Good, L. L., Laskowski, R. A., Pozzati, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00849-w · Cited by 675
Research works printed but not linked: 56
- 2017, Context-aware prediction of pathogenicity of missense mutations involved in human disease, arXiv preprint
- 10.1038/nbt.3769 · DOI · Paper page
- 2010, A method and server for predicting damaging missense mutations, Nature methods, 7, 248, 10.1038/nmeth0410-248 · DOI · Paper page
- 2018, Prediction and interpretation of deleterious coding variants in terms of protein structural stability, Scientific reports, 8, 4480, 10.1038/s41598-018-22531-2 · DOI
- 10.1186/1471-2105-12-1 · DOI
- 2020, Rhapsody: predicting the pathogenicity of human missense variants, Bioinformatics, 36, 3084, 10.1093/bioinformatics/btaa127 · DOI
- 2023, Predicting the pathogenicity of missense variants using features derived from AlphaFold2, Bioinformatics, 39, btad280, 10.1093/bioinformatics/btad280 · DOI · Paper page
- 2018, Structural dynamics is a determinant of the functional significance of missense variants, Biophysical Journal, 114, 232a, 10.1016/j.bpj.2017.11.1291 · DOI
- 10.1093/bib/bbz146 · DOI
- 10.1016/S0022-2836(02)00813-6 · DOI
- 2017, Role of structural bioinformatics in drug discovery by computational SNP analysis: analyzing variation at the protein level, Global heart, 12, 151, 10.1016/j.gheart.2017.01.009 · DOI
- 2017, Structure-based analysis of single nucleotide variants in the renin-angiotensinogen complex, Global Heart, 12, 121, 10.1016/j.gheart.2017.01.006 · DOI
- 10.1016/j.jmb.2021.167180 · DOI · Paper page
- 10.1016/j.drudis.2017.08.004 · DOI
- 2020, High accuracy protein structure prediction using deep learning, Fourteenth critical assessment of techniques for protein structure prediction (abstract book), 22, 2
- 10.1093/NAR/GKAB1061 · DOI · Paper page
- 10.1093/nar/gkab1061 · DOI · Paper page
- 2021, Highly accurate protein structure prediction for the human proteome, Nature, 596, 590, 10.1038/s41586-021-03828-1 · DOI · Paper page
- 10.1002/pmic.202200128 · DOI
- Peng K , Obradovic Z , Vucetic S. Exploring bias in the Protein Data Bank using contrast classifiers. In: Biocomputing 2004. World Scientific; 2003. p. 435–446. · DOI
- 2018, Gene annotation bias impedes biomedical research, Scientific reports, 8, 1362, 10.1038/s41598-018-19333-x · DOI · Paper page
- 2023, Accurate proteome-wide missense variant effect prediction with AlphaMissense, Science, 381, eadg7492, 10.1126/science.adg7492 · DOI · Paper page
- 10.1093/nar/gkx1153 · DOI · Paper page
- 10.1093/nar/gky1049 · DOI · Paper page
- 10.1093/nar/gkf493 · DOI
- 10.1093/protein/12.5.387 · DOI
- 10.1016/0022-2836(82)90515-0 · DOI
- 10.1016/0022-2836(74)90570-1 · DOI
- 10.1073/pnas.89.22.10915 · DOI · Paper page
- 1994, Conservation and prediction of solvent accessibility in protein families, Proteins: Structure, Function, and Bioinformatics, 20, 216, 10.1002/prot.340200303 · DOI
- 10.1371/journal.pone.0080635 · DOI
- 10.1016/0022-2836(87)90038-6 · DOI
- 10.1093/bioinformatics/btp163 · DOI · Paper page
- Chen T , Guestrin C. Xgboost: A scalable tree boosting system. In: Proceedings of the 22nd acm sigkdd international conference on knowledge discovery and data mining; 2016. p. 785–794. · DOI · Paper page
- Bergstra J , Yamins D , Cox D. Making a science of model search: Hyperparameter optimization in hundreds of dimensions for vision architectures. In: International conference on machine learning. PMLR; 2013. p. 115–123.
- 10.1093/nar/gkq603 · DOI
- 10.1038/s41587-022-01316-z · DOI
- 10.1371/journal.pbio.2006643 · DOI · Paper page
- 10.1038/470163a · DOI · Paper page
- 2015, Missing strings of residues in protein crystal structures, Intrinsically disordered proteins, 3, e1095697, 10.1080/21690707.2015.1095697 · DOI
- 10.1093/bioinformatics/btt473 · DOI · Paper page
- 2014, Cross-validation pitfalls when selecting and assessing regression and classification models, Journal of cheminformatics, 6, 1
- 10.1002/humu.22768 · DOI · Paper page
- Zhou Y , Tremmel R , Schaeffeler E , Schwab M , Lauschke VM . Challenges and opportunities associated with rare-variant pharmacogenomics. Trends in Pharmacological Sciences. 2022;. · DOI
- Sundararajan M , Najmi A. The many Shapley values for model explanation. In: International conference on machine learning. PMLR; 2020. p. 9269–9278.
- 2013, Predicting functional effect of human missense mutations using PolyPhen-2, Current protocols in human genetics, 76, 7
- 2023, Evaluation of AlphaFold structure-based protein stability prediction on missense variations in cancer, Frontiers in Genetics, 14, 1052383, 10.3389/fgene.2023.1052383 · DOI
- 10.1016/j.ajhg.2018.08.005 · DOI
- 10.1186/s12864-020-6490-7 · DOI
- 2020, On the performance of Matthews correlation coefficient (MCC) for imbalanced dataset, Pattern Recognition Letters, 136, 71, 10.1016/j.patrec.2020.03.030 · DOI
- 2021, PTP-MEG2 regulates quantal size and fusion pore opening through two distinct structural bases and substrates, EMBO reports, 22, e52141, 10.15252/embr.202052141 · DOI
- 10.1038/386569a0 · DOI · Paper page
- 10.1021/bi0602718 · DOI · Paper page
- 10.1002/humu.21656 · DOI
- 10.1002/pro.3667 · DOI
- 2018, Proteome-wide comparison between the amino acid composition of domains and linkers, BMC research notes, 11, 1
Metadata
- Authors
- Pir, M. S., & Timucin, E.
- Affiliations
- Acıbadem University (TR)
- Venue
- Protein Science
- Publisher
- openRxiv
- Published
- 2024-05-15
- Volume
- 34
- Issue
- 2
- Pages
- e70030-e70030
- ISSN
- 0961-8368 (ISSN-L)
- PMC
- PMC11751861
- OpenAlex
- W4406702706
- Cited by
- 0
- References
- 2
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- green
- pmc.ncbi.nlm.nih.gov
- Locations
- Protein Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- AlphaFold2, protein structure-based prediction, solvent accessibility, protein structure prediction, human proteome, functional impact prediction
- MeSH terms
- Machine Learning, Humans, Models, Molecular, Protein Conformation, Proteins, Software, Computational Biology, Mutation, Missense, Databases, Protein
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