期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 28, 页码 7364-7367出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201403694
关键词
FG-nucleoporin; fluorescence; intrinsically disordered proteins; ligand binding; multivalency
资金
- Boehringer Ingelheim fonds
- Emmy Noether program of the DFG
Intrinsically disordered proteins (IDPs) can bind to multiple interaction partners. Numerous binding regions in the IDP that act in concert through complex cooperative effects facilitate such interactions, but complicate studying IDP complexes. To address this challenge we developed a combined fluorescence correlation and time-resolved polarization spectroscopy approach to study the binding properties of the IDP nucleoporin153 (Nup153) to nuclear transport receptors (NTRs). The detection of segmental backbone mobility of Nup153 within the unperturbed complex provided a readout of local, region-specific binding properties that are usually masked in measurements of the whole IDP. The binding affinities of functionally and structurally diverse NTRs to distinct regions of Nup153 can differ by orders of magnitudes-a result with implications for the diversity of transport routes in nucleocytoplasmic transport.
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