Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Structural basis for cooperativity of CRM1 export complex formation.

Monecke, T., Haselbach, D., Voß, D., Russek, A., Neumann, P., Thomson, E., et al. (2013). Structural basis for cooperativity of CRM1 export complex formation. Proceedings of the National Academy of Sciences of the United States of America, 110(3), 960-965. doi:10.1073/pnas.1215214110.

Item is

Dateien

einblenden: Dateien
ausblenden: Dateien
:
1690406.pdf (Verlagsversion), 2MB
Name:
1690406.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-
:
1690406-Suppl-1.pdf (Ergänzendes Material), 5MB
Name:
1690406-Suppl-1.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-
:
1690406-Suppl-2.mp4 (Ergänzendes Material), 8MB
Name:
1690406-Suppl-2.mp4
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
video/x-msvideo / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-
:
1690406-Suppl-3.mp4 (Ergänzendes Material), 9MB
Name:
1690406-Suppl-3.mp4
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
video/x-msvideo / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:
ausblenden:
externe Referenz:
http://www.pnas.org/content/110/3/960.full.pdf+html (Verlagsversion)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Monecke, T., Autor
Haselbach, D.1, Autor           
Voß, D., Autor
Russek, A., Autor
Neumann, P., Autor
Thomson, E., Autor
Hurt, E., Autor
Zachariae, U., Autor
Stark, H.1, Autor           
Grubmüller, H.2, Autor           
Dickmanns, A., Autor
Ficner, R, Autor
Affiliations:
1Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              
2Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-β superfamily termed importins and exportins. The highly versatile exportin chromosome region maintenance 1 (CRM1) is essential for nuclear depletion of numerous structurally and functionally unrelated protein and ribonucleoprotein cargoes. CRM1 has been shown to adopt a toroidal structure in several functional transport complexes and was thought to maintain this conformation throughout the entire nucleocytoplasmic transport cycle. We solved crystal structures of free CRM1 from the thermophilic eukaryote Chaetomium thermophilum. Surprisingly, unbound CRM1 exhibits an overall extended and pitched superhelical conformation. The two regulatory regions, namely the acidic loop and the C-terminal α-helix, are dramatically repositioned in free CRM1 in comparison with the ternary CRM1–Ran–Snurportin1 export complex. Single-particle EM analysis demonstrates that, in a noncrystalline environment, free CRM1 exists in equilibrium between extended, superhelical and compact, ring-like conformations. Molecular dynamics simulations show that the C-terminal helix plays an important role in regulating the transition from an extended to a compact conformation and reveal how the binding site for nuclear export signals of cargoes is modulated by different CRM1 conformations. Combining these results, we propose a model for the cooperativity of CRM1 export complex assembly involving the long-range allosteric communication between the distant binding sites of GTP-bound Ran and cargo.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2012-12-312013-01-15
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.1215214110
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Proceedings of the National Academy of Sciences of the United States of America
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 110 (3) Artikelnummer: - Start- / Endseite: 960 - 965 Identifikator: -