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The structure of human argonaute-2 in complex with miR-20a


Elkayam, Elad ; Kuhn, Claus-D. ; Tocilj, Ante ; Haase, Astrid D. ; Greene, Emily M. ; Hannon, Gregory J. ; Joshua-Tor, Leemor:
The structure of human argonaute-2 in complex with miR-20a.
In: Cell. Bd. 150 (2012) Heft 1 . - S. 100-110.
ISSN 0092-8674
DOI: https://doi.org/10.1016/j.cell.2012.05.017


Link zum Volltext (externe URL): Volltext


Argonaute proteins lie at the heart of the RNA-induced silencing complex (RISC), wherein they use small RNA guides to recognize targets. Initial insight into the architecture of Argonautes came from studies of prokaryotic proteins, revealing a crescent-shaped base made up of the amino-terminal, PAZ, middle, and PIWI domains. The recently reported crystal structure of human Argonaute-2 (hAgo2), the "slicer" in RNA interference, in complex with a mixed population of RNAs derived from insect cells provides insight into the architecture of a eukaryotic Argonaute protein with defined biochemical and biological functions. Here, we report the structure of human Ago2 bound to a physiologically relevant microRNA, microRNA-20a, at 2.2 A resolution. The miRNA is anchored at both ends by the Mid and PAZ domains and makes several kinks and turns along the binding groove. Interestingly, miRNA binding confers remarkable stability on hAgo2, locking this otherwise flexible enzyme into a stable conformation.

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Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: Argonaute Proteins/*chemistry/isolation & purification/*metabolism; Crystallography, X-Ray; Humans; MicroRNAs/*chemistry/*metabolism; Models, Molecular; Protein Structure, Tertiary; Recombinant Proteins/chemistry/isolation & purification/metabolism
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Profilfelder > Advanced Fields > Molekulare Biowissenschaften
Forschungseinrichtungen > Forschungszentren > Bayreuther Zentrum für Molekulare Biowissenschaften - BZMB
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Profilfelder > Advanced Fields
Forschungseinrichtungen > Forschungszentren
Titel an der UBT entstanden: Nein
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
Eingestellt am: 10 Jan 2017 10:54
Letzte Änderung: 10 Jan 2017 10:54
URI: https://eref.uni-bayreuth.de/id/eprint/35639