Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains
Structural disorder is an essential ingredient for function in many proteins and protein complexes. Fuzzy complexes describe the many instances where disorder is maintained as a critical element of protein interactions. In this minireview we discuss how intramolecular fuzzy interactions function in...
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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2018-04-01
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Series: | Frontiers in Molecular Biosciences |
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Online Access: | http://journal.frontiersin.org/article/10.3389/fmolb.2018.00039/full |
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author | Miguel Arbesú Guillermo Iruela Héctor Fuentes João M. C. Teixeira Miquel Pons |
author_facet | Miguel Arbesú Guillermo Iruela Héctor Fuentes João M. C. Teixeira Miquel Pons |
author_sort | Miguel Arbesú |
collection | DOAJ |
description | Structural disorder is an essential ingredient for function in many proteins and protein complexes. Fuzzy complexes describe the many instances where disorder is maintained as a critical element of protein interactions. In this minireview we discuss how intramolecular fuzzy interactions function in signaling complexes. Focussing on the Src family of kinases, we argue that the intrinsically disordered domains that are unique for each of the family members and display a clear fingerprint of long range interactions in Src, might have critical roles as functional sensor or effectors and mediate allosteric communication via fuzzy interactions. |
first_indexed | 2024-12-13T14:10:10Z |
format | Article |
id | doaj.art-51796fc6c5c64fa5a3a1c01db2dd3060 |
institution | Directory Open Access Journal |
issn | 2296-889X |
language | English |
last_indexed | 2024-12-13T14:10:10Z |
publishDate | 2018-04-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Molecular Biosciences |
spelling | doaj.art-51796fc6c5c64fa5a3a1c01db2dd30602022-12-21T23:42:29ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2018-04-01510.3389/fmolb.2018.00039360170Intramolecular Fuzzy Interactions Involving Intrinsically Disordered DomainsMiguel ArbesúGuillermo IruelaHéctor FuentesJoão M. C. TeixeiraMiquel PonsStructural disorder is an essential ingredient for function in many proteins and protein complexes. Fuzzy complexes describe the many instances where disorder is maintained as a critical element of protein interactions. In this minireview we discuss how intramolecular fuzzy interactions function in signaling complexes. Focussing on the Src family of kinases, we argue that the intrinsically disordered domains that are unique for each of the family members and display a clear fingerprint of long range interactions in Src, might have critical roles as functional sensor or effectors and mediate allosteric communication via fuzzy interactions.http://journal.frontiersin.org/article/10.3389/fmolb.2018.00039/fullfuzzy complexesintrinsically disordered proteinsSrc family kinasesallosteryfuzzy domainsparamagnetic relaxation enhancement |
spellingShingle | Miguel Arbesú Guillermo Iruela Héctor Fuentes João M. C. Teixeira Miquel Pons Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains Frontiers in Molecular Biosciences fuzzy complexes intrinsically disordered proteins Src family kinases allostery fuzzy domains paramagnetic relaxation enhancement |
title | Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains |
title_full | Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains |
title_fullStr | Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains |
title_full_unstemmed | Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains |
title_short | Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains |
title_sort | intramolecular fuzzy interactions involving intrinsically disordered domains |
topic | fuzzy complexes intrinsically disordered proteins Src family kinases allostery fuzzy domains paramagnetic relaxation enhancement |
url | http://journal.frontiersin.org/article/10.3389/fmolb.2018.00039/full |
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