αα-Hub domains and intrinsically disordered proteins: A decisive combo
| Autor: | Rasmus Greve Falbe-Hansen, Birthe B. Kragelund, Lasse Staby, Karen Skriver, Katrine Bugge, Edoardo Salladini |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical 0301 basic medicine Protein Folding TF transcription factor Computer science NHR1 nervy homology region 1 Arabidopsis IDP HDAC histone deacetylase Cell Cycle Proteins Ligand Binding Protein CCM2 cerebral cavernous malformation 2 Biochemistry context Transcription Factors TFII RST RCD1 SRO and TAF4 HID HDAC interacting domain p300-CBP Transcription Factors PARP poly(ADP-ribose)polymerase SLiM biology ITC isothermal titration calorimetry dynamics RCD1 Radical-Induced Cell Death1 Ligand (biochemistry) MD molecular dynamics ID intrinsic structural disorder HHD harmonin homology domain Sin3 Histone Deacetylase and Corepressor Complex Histone fold TRD TF regulatory domain Motif (music) signaling transcription NCBD nuclear coactivator binding domain SLiM short linear motif Protein Binding HF histone-fold ligand binding CBP CREB binding protein Reviews Saccharomyces cerevisiae Computational biology Intrinsically disordered proteins TAFH TATA-box associated factor homology ETO eight-twenty-one 03 medical and health sciences Signal fidelity Animals Humans Protein Interaction Domains and Motifs Short linear motif CREB-binding protein Molecular Biology GO gene ontology TATA-Binding Protein Associated Factors PAH paired amphipathic helix Binding Sites 030102 biochemistry & molecular biology Arabidopsis Proteins hub Cell Biology AD activation domain RTEL1 regulator of telomere elongation helicase 1 Intrinsically Disordered Proteins IDR intrinsically disordered region Cytoskeletal Proteins 030104 developmental biology biology.protein Protein Conformation beta-Strand Transcription Factor TFIID TAF4 transcription initiation factor TFIID-subunit 4 Transcription Factors |
| Zdroj: | The Journal of Biological Chemistry Bugge, K, Staby, L, Salladini, E, Falbe-Hansen, R G, Kragelund, B B & Skriver, K 2021, ' αα-Hub domains and intrinsically disordered proteins : a decisive combo ', Journal of Biological Chemistry, vol. 296, 100226 . https://doi.org/10.1074/jbc.REV120.012928 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.rev120.012928 |
| Popis: | Hub proteins are central nodes in protein-protein interaction networks with critical importance to all living organisms. Recently, a new group of folded hub domains, the αα-hubs, was defined based on a shared αα-hairpin super-secondary structural foundation. The members PAH, RST, TAFH, NCBD and HHD are found in large proteins such as Sin3, RCD1, TAF4, CBP and harmonin, which organize disordered transcriptional regulators and membrane scaffolds in interactomes of importance to human diseases and plant quality. In this review, studies of structures, functions, and complexes across the αα-hubs are described and compared to provide a unified description of the group. This analysis expands the associated molecular concepts of "one domain - one superbinding site", motif-based ligand binding, and coupled folding and binding of intrinsically disordered ligands to additional concepts of importance to signal fidelity. These include context, motif reversibility, multivalency, complex heterogeneity, synergistic αα-hub:ligand folding, accessory binding-sites, and supramodules. We propose that these multifaceted protein-protein interaction properties are made possible by the characteristics of the αα-hub fold, including super-site properties, dynamics, variable topologies, accessory helices and malleability and abetted by adaptability of the disordered ligands. Critically, these features provide additional filters for specificity. With the presentations of new concepts, this review opens for new research questions addressing properties across the group, which are driven from concepts discovered in studies of the individual members. Combined, the members of the αα-hubs are ideal models for deconvoluting signal fidelity maintained by folded hubs and their interactions with intrinsically disordered ligands. |
| Databáze: | OpenAIRE |
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