ArticleJournal of molecular evolution2007
Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation.
Article in Journal of molecular evolution, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Evolution of an amphibian-specific family of epidermal differentiation-associated genes.Molecular biology and evolution · 2026Article
- Decoding intrinsically disordered regions in biomolecular condensates.Fundamental research · 2026Review
- An integrative multitiered computational analysis for better understanding the structure and function of 85 miniproteins.NAR genomics and bioinformatics · 2025Article
- Evolution of intrinsic disorder in the structural domains of viral and cellular proteomes.Scientific reports · 2025Article
- Fuzzy protein-DNA interactions and beyond: A common theme in transcription?Current opinion in structural biology · 2024Review
- Evolutionary analyses of intrinsically disordered regions reveal widespread signals of conservation.PLoS computational biology · 2024Article
- Sequence-independent activity of a predicted long disordered segment of the human papillomavirus type 16 L2 capsid protein during virus entry.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Evolution of Intrinsic Disorder in Protein Loops.Life (Basel, Switzerland) · 2023Article
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- The unstructured linker of Mlh1 contains a motif required for endonuclease function which is mutated in cancers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- DMFpred: Predicting protein disorder molecular functions based on protein cubic language model.PLoS computational biology · 2022Article
- Conformational buffering underlies functional selection in intrinsically disordered protein regions.Nature structural & molecular biology · 2022Article
- FG nucleoporins feature unique patterns that distinguish them from other IDPs.Biophysical journal · 2021Article
- Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex.eLife · 2020Article
- Evolutionary Forces and Codon Bias in Different Flavors of Intrinsic Disorder in the Human Proteome.Journal of molecular evolution · 2020Article
- IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions-Insights from transcription factors.Protein science : a publication of the Protein Society · 2020Article
- Intrinsically disordered domains: Sequence ➔ disorder ➔ function relationships.Protein science : a publication of the Protein Society · 2019Article
- Entropy and Information within Intrinsically Disordered Protein Regions.Entropy (Basel, Switzerland) · 2019Article
- Proteome-wide signatures of function in highly diverged intrinsically disordered regions.eLife · 2019Article
- Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Proteins or regions of proteins that do not form compact globular structures are classified as intrinsically unstructured proteins (IUPs). IUPs are common in nature and have essential molecular functions, but even a limited understanding of the evolution of their dynamic behavior is lacking. The primary objective of this work was to test the evolutionary conservation of dynamic behavior for a particular class of IUPs that form intrinsically unstructured linker domains (IULD) that tether flanking folded domains. This objective was accomplished by measuring the backbone flexibility of several IULD homologues using nuclear magnetic resonance (NMR) spectroscopy. The backbone flexibility of five IULDs, representing three kingdoms, was measured and analyzed. Two IULDs from animals, one IULD from fungi, and two IULDs from plants showed similar levels of backbone flexibility that were consistent with the absence of a compact globular structure. In contrast, the amino acid sequences of the IULDs from these three taxa showed no significant similarity. To investigate how the dynamic behavior of the IULDs could be conserved in the absence of detectable sequence conservation, evolutionary rate studies were performed on a set of nine mammalian IULDs. The results of this analysis showed that many sites in the IULD are evolving neutrally, suggesting that dynamic behavior can be maintained in the absence of natural selection. This work represents the first experimental test of the evolutionary conservation of dynamic behavior and demonstrates that amino acid sequence conservation is not required for the conservation of dynamic behavior and presumably molecular function.
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