Transient structural properties of the Rho GDP‐dissociation inhibitor

Simple item page
dc.contributor.authorMedina Gomez, Sara
dc.contributor.authorVisco, Ilaria
dc.contributor.authorMerino, Felipe
dc.contributor.authorBieling, Peter
dc.contributor.authorLinser, Rasmus
dc.date.accessioned2026-01-15T08:17:28Z
dc.date.available2026-01-15T08:17:28Z
dc.date.issued2024-06-09
dc.description.abstractRho GTPases, master spatial regulators of a wide range of cellular processes, are orchestrated by complex formation with guanine nucleotide dissociation inhibitors (RhoGDIs). These have been thought to possess an unstructured N-terminus that inhibits nucleotide exchange of their client upon binding/folding. Via NMR analyses, molecular dynamics simulations, and biochemical assays, we reveal instead pertinent structural properties transiently maintained both, in the presence and absence of the client, imposed onto the terminus context-specifically by modulating interactions with the surface of the folded C-terminal domain. These observations revise the long-standing textbook picture of the GTPases’ mechanism of membrane extraction. Rather than by a disorder-to-order transition upon binding of an inhibitory peptide, the intricate and highly selective extraction process of RhoGTPases is orchestrated via a dynamic ensemble bearing preformed transient structural properties, suitably modulated by the specific surrounding along the multi-step process.en
dc.identifier.urihttp://hdl.handle.net/2003/44677
dc.language.isoen
dc.relation.ispartofseriesAngewandte Chemie / International edition; 63(34)
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectRhoGTPasesen
dc.subjectNMR spectroscopyen
dc.subjectProtein dynamicsen
dc.subjectProtein complexesen
dc.subjectConformational disorderen
dc.subject.ddc540
dc.subject.rswkRho-Proteine
dc.subject.rswkNMR-Spektroskopie
dc.subject.rswkMultiproteinkomplex
dc.subject.rswkMolekularbewegung
dc.subject.rswkKonformation
dc.titleTransient structural properties of the Rho GDP‐dissociation inhibitoren
dc.typeText
dc.type.publicationtypeResearchArticle
dcterms.accessRightsopen access
eldorado.dnb.deposittrue
eldorado.doi.registerfalse
eldorado.openaire.projectidentifierinfo:eu-repo/grantAgreement/EC/HE/101082494/EU/Fast-MAS Solid-State NMR as a Bypass to High-Molecular-Weight Proteins in Solution/bypassNMR/
eldorado.secondarypublicationtrue
eldorado.secondarypublication.primarycitationS. Medina Gomez, I. Visco, F. Merino, P. Bieling, R. Linser, Angew. Chem. Int. Ed. 2024, 63, e202403941. https://doi.org/10.1002/anie.202403941
eldorado.secondarypublication.primaryidentifierhttps://doi.org/10.1002/anie.202403941

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Angew Chem Int Ed - 2024 - Medina Gomez - Transient Structural Properties of the Rho GDP‐Dissociation Inhibitor.pdf
Size:
2.48 MB
Format:
Adobe Portable Document Format
Description:
DNB
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
4.82 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

Physikalische Chemie