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Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions.

dc.contributor.author Coutavas, Elias
dc.contributor.author Blus, Bartlomiej Jan
dc.contributor.author Koh, Junseock
dc.contributor.author Krolak, Aleksandra
dc.contributor.author Seo, Hyuk-Soo
dc.contributor.author Blobel, Günter
dc.date.accessioned 2020-02-13T20:49:29Z
dc.date.available 2020-02-13T20:49:29Z
dc.date.issued 2019-11-27
dc.identifier aax1836
dc.identifier.issn 2375-2548
dc.identifier.issn 2375-2548
dc.identifier.uri https://hdl.handle.net/10161/20158
dc.description.abstract Intrinsically disordered regions (IDRs) of proteins are implicated in key macromolecular interactions. However, the molecular forces underlying IDR function within multicomponent assemblies remain elusive. By combining thermodynamic and structural data, we have discovered an allostery-based mechanism regulating the soluble core region of the nuclear pore complex (NPC) composed of nucleoporins Nup53, Nic96, and Nup157. We have identified distinct IDRs in Nup53 that are functionally coupled when binding to partner nucleoporins and karyopherins (Kaps) involved in NPC assembly and nucleocytoplasmic transport. We show that the Nup53·Kap121 complex forms an ensemble of structures that destabilize Nup53 hub interactions. Our study provides a molecular framework for understanding how disordered and folded domains communicate within macromolecular complexes.
dc.language eng
dc.publisher American Association for the Advancement of Science (AAAS)
dc.relation.ispartof Science advances
dc.relation.isversionof 10.1126/sciadv.aax1836
dc.subject Science & Technology
dc.subject Multidisciplinary Sciences
dc.subject Science & Technology - Other Topics
dc.subject NUCLEAR-PORE COMPLEX
dc.subject STRUCTURAL BASIS
dc.subject MOLECULAR ARCHITECTURE
dc.subject INNER RING
dc.subject PROTEINS
dc.subject TITRATION
dc.subject BINDING
dc.subject DNA
dc.subject KAP121P
dc.subject CHANNEL
dc.title Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions.
dc.type Journal article
duke.contributor.id Coutavas, Elias|1029255
dc.date.updated 2020-02-13T20:49:25Z
pubs.begin-page eaax1836
pubs.issue 11
pubs.organisational-group School of Medicine
pubs.organisational-group Medicine, Pulmonary, Allergy, and Critical Care Medicine
pubs.organisational-group Duke
pubs.organisational-group Medicine
pubs.organisational-group Clinical Science Departments
pubs.publication-status Published
pubs.volume 5
duke.contributor.orcid Coutavas, Elias|0000-0003-4904-0081


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