When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes
The degree of proteins structural organization ranges from highly structured, compact folding to intrinsic disorder, where each degree of self-organization corresponds to specific functions: well-organized structural motifs in enzymes offer a proper environment for precisely positioned functional gr...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-10-01
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| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/11/10/1529 |
| _version_ | 1797515229027893248 |
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| author | Sophie Sacquin-Mora Chantal Prévost |
| author_facet | Sophie Sacquin-Mora Chantal Prévost |
| author_sort | Sophie Sacquin-Mora |
| collection | DOAJ |
| description | The degree of proteins structural organization ranges from highly structured, compact folding to intrinsic disorder, where each degree of self-organization corresponds to specific functions: well-organized structural motifs in enzymes offer a proper environment for precisely positioned functional groups to participate in catalytic reactions; at the other end of the self-organization spectrum, intrinsically disordered proteins act as binding hubs via the formation of multiple, transient and often non-specific interactions. This review focusses on cases where structurally organized proteins or domains associate with highly disordered protein chains, leading to the formation of interfaces with varying degrees of fuzziness. We present a review of the computational methods developed to provide us with information on such fuzzy interfaces, and how they integrate experimental information. The discussion focusses on two specific cases, microtubules and homologous recombination nucleoprotein filaments, where a network of intrinsically disordered tails exerts regulatory function in recruiting partner macromolecules, proteins or DNA and tuning the atomic level association. Notably, we show how computational approaches such as molecular dynamics simulations can bring new knowledge to help bridging the gap between experimental analysis, that mostly concerns ensemble properties, and the behavior of individual disordered protein chains that contribute to regulation functions. |
| first_indexed | 2024-03-10T06:42:33Z |
| format | Article |
| id | doaj.art-859cf5efbbc8429d8c172d8fbfee0009 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T06:42:33Z |
| publishDate | 2021-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-859cf5efbbc8429d8c172d8fbfee00092023-11-22T17:35:01ZengMDPI AGBiomolecules2218-273X2021-10-011110152910.3390/biom11101529When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy ComplexesSophie Sacquin-Mora0Chantal Prévost1CNRS, Laboratoire de Biochimie Théorique, UPR9080, Université de Paris, 13 Rue Pierre et Marie Curie, 75005 Paris, FranceCNRS, Laboratoire de Biochimie Théorique, UPR9080, Université de Paris, 13 Rue Pierre et Marie Curie, 75005 Paris, FranceThe degree of proteins structural organization ranges from highly structured, compact folding to intrinsic disorder, where each degree of self-organization corresponds to specific functions: well-organized structural motifs in enzymes offer a proper environment for precisely positioned functional groups to participate in catalytic reactions; at the other end of the self-organization spectrum, intrinsically disordered proteins act as binding hubs via the formation of multiple, transient and often non-specific interactions. This review focusses on cases where structurally organized proteins or domains associate with highly disordered protein chains, leading to the formation of interfaces with varying degrees of fuzziness. We present a review of the computational methods developed to provide us with information on such fuzzy interfaces, and how they integrate experimental information. The discussion focusses on two specific cases, microtubules and homologous recombination nucleoprotein filaments, where a network of intrinsically disordered tails exerts regulatory function in recruiting partner macromolecules, proteins or DNA and tuning the atomic level association. Notably, we show how computational approaches such as molecular dynamics simulations can bring new knowledge to help bridging the gap between experimental analysis, that mostly concerns ensemble properties, and the behavior of individual disordered protein chains that contribute to regulation functions.https://www.mdpi.com/2218-273X/11/10/1529intrinsically disordered proteinsmolecular modelingfuzzy complexesdisorder and function |
| spellingShingle | Sophie Sacquin-Mora Chantal Prévost When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes Biomolecules intrinsically disordered proteins molecular modeling fuzzy complexes disorder and function |
| title | When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes |
| title_full | When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes |
| title_fullStr | When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes |
| title_full_unstemmed | When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes |
| title_short | When Order Meets Disorder: Modeling and Function of the Protein Interface in Fuzzy Complexes |
| title_sort | when order meets disorder modeling and function of the protein interface in fuzzy complexes |
| topic | intrinsically disordered proteins molecular modeling fuzzy complexes disorder and function |
| url | https://www.mdpi.com/2218-273X/11/10/1529 |
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