ArticlePLoS computational biology2018
Same but not alike: Structure, flexibility and energetics of domains in multi-domain proteins are influenced by the presence of other domains.
Article in PLoS computational biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 54 citations in OpenAlex.
- Integrated analysis with iCM-SANS, SAXS and MD simulations for dynamics of multi-domain proteins.Journal of applied crystallography · 2026Article
- Domain arrangement-driven immunogenicity of a computationally designed mRNA vaccine targeting PPE68, IrtA, and PE9 of Mycobacterium tuberculosis.Scientific reports · 2026Article
- Molecular Mimicry Inference, Therapeutic Target Identification, and Natural Product Inhibition Study inACS omega · 2026Article
- Genome-wide identification and characterization of SET domain family genes in Neopyropia yezoensis.BMC genomics · 2026Article
- Hydrophobic residues in the D-domain of a plasminogen-binding M-protein modulate α-helicity, oligomerization, and surface anchoring in Streptococcus pyogenes.Protein science : a publication of the Protein Society · 2025Article
- Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.Angewandte Chemie (International ed. in English) · 2025Article
- Intrinsic Disorder and Other Malleable Arsenals of Evolved Protein Multifunctionality.Journal of molecular evolution · 2024Review
- Cooperative nucleic acid binding by Poly ADP-ribose polymerase 1.Scientific reports · 2024Article
- Dissection of the role of a Src homology 3 domain in the evolution of binding preference of paralogous proteins.Genetics · 2024Article
- Isothermal chemical denaturation assay for monitoring protein stability and inhibitor interactions.Scientific reports · 2023Article
- Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.Nature communications · 2023Article
- Unified access to up-to-date residue-level annotations from UniProtKB and other biological databases for PDB data.Scientific data · 2023Article
- Determinants of affinity, specificity, and phase separation in a supramodule from Post-synaptic density protein 95.iScience · 2022Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Probing ion channel functional architecture and domain recombination compatibility by massively parallel domain insertion profiling.Nature communications · 2021Article
- Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance.Journal of the American Chemical Society · 2021Article
- Decoding LncRNAs.Cancers · 2021Review
- Tethering-induced destabilization and ATP-binding for tandem RRM domains of ALS-causing TDP-43 and hnRNPA1.Scientific reports · 2021Article
- Exploring Large Domain Motions in Proteins Using Atomistic Molecular Dynamics with Enhanced Conformational Sampling.International journal of molecular sciences · 2020Article
- Allosteric cooperation in a de novo-designed two-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of the proteins encoded in the genomes of eukaryotes contain more than one domain. Reasons for high prevalence of multi-domain proteins in various organisms have been attributed to higher stability and functional and folding advantages over single-domain proteins. Despite these advantages, many proteins are composed of only one domain while their homologous domains are part of multi-domain proteins. In the study presented here, differences in the properties of protein domains in single-domain and multi-domain systems and their influence on functions are discussed. We studied 20 pairs of identical protein domains, which were crystallized in two forms (a) tethered to other proteins domains and (b) tethered to fewer protein domains than (a) or not tethered to any protein domain. Results suggest that tethering of domains in multi-domain proteins influences the structural, dynamic and energetic properties of the constituent protein domains. 50% of the protein domain pairs show significant structural deviations while 90% of the protein domain pairs show differences in dynamics and 12% of the residues show differences in the energetics. To gain further insights on the influence of tethering on the function of the domains, 4 pairs of homologous protein domains, where one of them is a full-length single-domain protein and the other protein domain is a part of a multi-domain protein, were studied. Analyses showed that identical and structurally equivalent functional residues show differential dynamics in homologous protein domains; though comparable dynamics between in-silico generated chimera protein and multi-domain proteins were observed. From these observations, the differences observed in the functions of homologous proteins could be attributed to the presence of tethered domain. Overall, we conclude that tethered domains in multi-domain proteins not only provide stability or folding advantages but also influence pathways resulting in differences in function or regulatory properties.
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