Journal
STRUCTURE
Volume 26, Issue 3, Pages 477-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2018.01.010
Keywords
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Funding
- NIH [GM117212, GM112108]
- Biomedical Technology Research Center for Multiscale Modeling of Biological Systems (MMBioS) from the NIH [P41GM103712-S1]
- NSF [ACI-105375]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM112108, P41GM109824, P41GM103712, R01GM117212] Funding Source: NIH RePORTER
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The largely intrinsically disordered phenylalanineglycine-rich nucleoporins (FG Nups) underline a selectivity mechanism that enables the rapid translocation of transport factors (TFs) through the nuclear pore complexes (NPCs). Conflicting models of NPC transport have assumed that FG Nups undergo different conformational transitions upon interacting with TFs. To selectively characterize conformational changes in FG Nups induced by TFs we performed small-angle neutron scattering (SANS) with contrast matching. Conformational-ensembles derived from SANS data indicated an increase in the overall size of FG Nups is associated with TF interaction. Moreover, the organization of the FG motif in the interacting state is consistent with prior experimental analyses defining that FG motifs undergo conformational restriction upon interacting with TFs. These results provide structural insights into a highly dynamic interaction and illustrate how functional disorder imparts rapid and selective FG Nup-TF interactions.
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