Miskei, Marton and Horvath, Attila and Vendruscolo, Michele and Fuxreiter, Monika (2020) Sequence-Based Prediction of Fuzzy Protein Interactions. JOURNAL OF MOLECULAR BIOLOGY, 432 (7). 2289 - 2303. ISSN 0022-2836
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Abstract
It is becoming increasingly recognised that disordered proteins may be fuzzy, in that they can exhibit a wide variety of binding modes. In addition to the well-known process of folding upon binding (disorder-to-order transition), many examples are emerging of interacting proteins that remain disordered in their bound states (disorder-to-disorder transitions). Furthermore, disordered proteins may populate ordered and disordered states to different extents depending on their partners (context-dependent binding). Here we assemble three datasets comprising disorder-to-order, context-dependent, and disorder-to-disorder transitions of 828 protein regions represented in 2157 complexes and elucidate the sequence-determinants of the different interaction modes. We found that fuzzy interactions originate from local sequence compositions that promote the sampling of a wide range of different structures. Based on this observation, we developed the FuzPred method (http://protdyn-fuzpred.org) of predicting the binding modes of disordered proteins based on their amino acid sequences, without specifying their partners. We thus illustrate how the amino acid sequences of proteins can encode a wide range of conformational changes upon binding, including transitions from disordered to ordered and from disordered to disordered states.
Item Type: | Article |
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Uncontrolled Keywords: | fuzzy interactions, disordered proteins, protein binding, fuzzy complexes, folding upon binding |
Subjects: | Q Science / természettudomány > Q1 Science (General) / természettudomány általában |
Depositing User: | Dr. Márton Miskei |
Date Deposited: | 22 Sep 2020 09:43 |
Last Modified: | 03 Apr 2023 06:57 |
URI: | http://real.mtak.hu/id/eprint/113902 |
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