Mechanism of Dis3l2 substrate recognition in the Lin28–let-7 pathway

Christopher R. Faehnle, Jack Walleshauser and Leemor Joshua-Tor ()
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Christopher R. Faehnle: W. M. Keck Structural Biology Laboratory, 1 Bungtown Road
Jack Walleshauser: W. M. Keck Structural Biology Laboratory, 1 Bungtown Road
Leemor Joshua-Tor: W. M. Keck Structural Biology Laboratory, 1 Bungtown Road

Nature, 2014, vol. 514, issue 7521, 252-256

Abstract: The structure of mouse Dis3l2 bound to an oligoU substrate shows a funnel-like substrate-binding site with the RNA being fed into the active site along a path that is distinct from that seen in the related catalytic subunit of the exosome — 12 uracils of the oligoU-tailed RNA are recognized in a complex network of interactions, suggesting the basis for target specificity.

Date: 2014
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DOI: 10.1038/nature13553

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