Emergence and evolution of an interaction between intrinsically disordered proteins
| العنوان: | Emergence and evolution of an interaction between intrinsically disordered proteins |
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| المؤلفون: | Per Jemth, Greta Hultqvist, Eva Andersson, Gustav N. Sundell, Carlo Camilloni, Jakob Dogan, Emma Åberg, Celestine N. Chi, Michele Vendruscolo |
| المصدر: | eLife, 6 eLife eLife, Vol 6 (2017) |
| بيانات النشر: | eLife Sciences Publications, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, Magnetic Resonance Spectroscopy, QH301-705.5, Evolution, Science, Systems biology, Protein domain, Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy), Plasma protein binding, Biology, Intrinsically disordered proteins, General Biochemistry, Genetics and Molecular Biology, Protein–protein interaction, Evolution, Molecular, 03 medical and health sciences, Protein-protein interaction, Protein Domains, Molecular evolution, None, Animals, Protein Interaction Maps, Biology (General), Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci), Organism, Genetics, General Immunology and Microbiology, General Neuroscience, phylogenetic reconstruction, General Medicine, Biophysics and Structural Biology, molecular dynamics, Intrinsically Disordered Proteins, 030104 developmental biology, Structural biology, Affinity, Evolutionary biology, Medicine, Protein Binding, Research Article, Computational and Systems Biology |
| الوصف: | Protein-protein interactions involving intrinsically disordered proteins are important for cellular function and common in all organisms. However, it is not clear how such interactions emerge and evolve on a molecular level. We performed phylogenetic reconstruction, resurrection and biophysical characterization of two interacting disordered protein domains, CID and NCBD. CID appeared after the divergence of protostomes and deuterostomes 450–600 million years ago, while NCBD was present in the protostome/deuterostome ancestor. The most ancient CID/NCBD formed a relatively weak complex (Kd∼5 µM). At the time of the first vertebrate-specific whole genome duplication, the affinity had increased (Kd∼200 nM) and was maintained in further speciation. Experiments together with molecular modeling using NMR chemical shifts suggest that new interactions involving intrinsically disordered proteins may evolve via a low-affinity complex which is optimized by modulating direct interactions as well as dynamics, while tolerating several potentially disruptive mutations. eLife, 6 ISSN:2050-084X |
| وصف الملف: | application/application/pdf; application/pdf |
| اللغة: | English |
| تدمد: | 2050-084X |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfc80f8e60608a1b96a231fd38d5e638Test https://hdl.handle.net/20.500.11850/191573Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....cfc80f8e60608a1b96a231fd38d5e638 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 2050084X |
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