Results 21 to 30 of about 29,703 (304)

Many-to-one binding by intrinsically disordered protein regions [PDF]

Biocomputing 2020, 2019
Disordered binding regions (DBRs), which are embedded within intrinsically disordered proteins or regions (IDPs or IDRs), enable IDPs or IDRs to mediate multiple protein-protein interactions. DBR-protein complexes were collected from the Protein Data Bank for which two or more DBRs having different amino acid sequences bind to the same (100% sequence ...
Alterovitz, Wei-Lun, Faraggi, Eshel, Oldfield, Christopher J., Meng, Jingwei, Xue, Bin, Huang, Fei, Romero, Pedro, Kloczkowski, Andrzej, Uversky, Vladimir N., Dunker, A. Keith   +9 more
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Classification of Intrinsically Disordered Regions and Proteins

Chemical Reviews, 2014
1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences ...
Van Der Lee R., Buljan M., Lang B., Weatheritt R. J., Daughdrill G. W., Dunker A. K., Fuxreiter M., Gough J., Gsponer J., Jones D. T., Kim P. M., Kriwacki R. W., Oldfield C. J., Pappu R. V., Tompa P., Uversky V. N., Wright P. E., Babu M. M.   +17 more
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Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions

Biomolecules, 2022
Intrinsically disordered regions (IDRs) carry out many cellular functions and vary in length and placement in protein sequences. This diversity leads to variations in the underlying compositional biases, which were demonstrated for the short vs. long IDRs. We analyze compositional biases across four classes of disorder: fully disordered proteins; short
Bi Zhao, Lukasz Kurgan
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Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins [PDF]

Protein Science, 2019
AbstractPhosphorylation is a major post‐translational modification that plays a central role in signaling pathways. Protein kinases phosphorylate substrates (phosphoproteins) by adding phosphate at Ser/Thr or Tyr residues (phosphosites). A large amount of data identifying and describing phosphosites in phosphoproteins has been reported but the ...
Ryotaro Koike, Mutsuki Amano, Kozo Kaibuchi, Motonori Ota   +3 more
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Entropy and Information within Intrinsically Disordered Protein Regions [PDF]

Entropy, 2019
Bioinformatics and biophysical studies of intrinsically disordered proteins and regions (IDRs) note the high entropy at individual sequence positions and in conformations sampled in solution. This prevents application of the canonical sequence-structure-function paradigm to IDRs and motivates the development of new methods to extract information from ...
Iva Pritisanac, Robert M. Vernon, Alan M. Moses, Julie D. Forman-Kay   +3 more
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Intrinsically disordered regions in TRPV2 mediate protein-protein interactions

Communications Biology, 2023
AbstractTransient receptor potential (TRP) ion channels are gated by diverse intra- and extracellular stimuli leading to cation inflow (Na+, Ca2+) regulating many cellular processes and initiating organismic somatosensation. Structures of most TRP channels have been solved.
Sanganna Gari, Raghavendar, Tagiltsev, Grigory, Pumroy, Ruth, Jiang, Yining, Blackledge, Martin, Moiseenkova-Bell, Vera, Scheuring, Simon   +6 more
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On the roles of intrinsically disordered proteins and regions in cell communication and signaling [PDF]

Cell Communication and Signaling, 2021
AbstractFor proteins, the sequence → structure → function paradigm applies primarily to enzymes, transmembrane proteins, and signaling domains. This paradigm is not universal, but rather, in addition to structured proteins, intrinsically disordered proteins and regions (IDPs and IDRs) also carry out crucial biological functions. For these proteins, the
Bondos, Sarah E., Dunker, A. Keith, Uversky, Vladimir N.   +2 more
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Analysis of structured and intrinsically disordered regions of transmembrane proteins [PDF]

Molecular BioSystems, 2009
Abstract Integral membraneproteins display two major types of transmembrane structure, helical bundles and beta barrels. The main functional roles of transmembrane proteins are the transport of small molecules and cellsignaling, and sometimes these two roles are coupled.
Xue, Bin, Li, Liwei, Meroueh, Samy O., Uversky, Vladimir N., Dunker, A. Keith   +4 more
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The tail of cryptochromes: an intrinsically disordered cog within the mammalian circadian clock

Cell Communication and Signaling, 2020
Cryptochrome (CRY) proteins play an essential role in regulating mammalian circadian rhythms. CRY is composed of a structured N-terminal domain known as the photolyase homology region (PHR), which is tethered to an intrinsically disordered C-terminal ...
Gian Carlo G. Parico, Carrie L. Partch
doaj   +1 more source

Evolutionary fine-tuning of residual helix structure in disordered proteins manifests in complex structure and lifetime

Communications Biology, 2023
Evolution-guided mutagenesis and biophysical analysis reveal that residual helical structure in the binding region of an intrinsically disordered protein regulates the lifetime of its complex by affecting its dissociation.
Steffie Elkjær, Amanda D. Due, Lise F. Christensen, Frederik F. Theisen, Lasse Staby, Birthe B. Kragelund, Karen Skriver   +6 more
doaj   +1 more source