Karyopherin flexibility in nucleocytoplasmic transport
Abstract
Recent structural work on nuclear transport factors of the importin-beta superfamily of karyopherins has shown that these proteins are superhelices of HEAT repeats that are able to assume different conformations in different functional states. The inherent flexibility of these helicoids facilitates the accommodation of different binding partners by an induced-fit type of mechanism. Moreover, the energy stored by distorting these molecules may partially balance binding energies to enable assembly and disassembly of their complexes with relatively small energy changes. Flexibility appears to be an intrinsic feature of such superhelices and might be functionally important not only for karyopherins and nuclear transport, but also for HEAT repeat proteins from other biological systems.
Read the paper
Related studies
- The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
- X-ray-Computed Tomography Contrast Agents
- Reactivity of Surface Species in Heterogeneous Catalysts Probed by In Situ X-ray Absorption Techniques
- Single-crystal X-ray diffraction studies on structural transformations of porous coordination polymers
- Investigation of solid/vapor interfaces using ambient pressure X-ray photoelectron spectroscopy
- Resonant X-Ray Scattering Studies of Charge Order in Cuprates
Go deeper in Evidence Hub
Evidence Hub adds a study data sheet (design, sample size, evidence level, key numbers), an AI summary and a chat grounded in the paper's text.