TY - JOUR
T1 - Binding dynamics of isolated nucleoporin repeat regions to importin-β
AU - Isgro, Timothy A.
AU - Schulten, Klaus
N1 - Funding Information:
The authors would like to thank Yi Wang for her help in equilibrating the transport complex system as well as for her continuous input throughout the project. The authors would also like to thank Dr. Frank Alber for thought-provoking discussions on simulating nucleoporins in general and FG-Nups in particular. Finally, the authors would like to thank Zan Luthey-Schulten and coworkers for the development of the VMD Multiple Alignment plugin for structural and sequence alignment of proteins. The work was supported by the National Institutes of Health grant P41-RR05969. Computer time was provided by the National Science Foundation through the National Resource Allocation Committee grant MCA93S028. All molecular images in this paper were prepared by using the molecular visualization software VMD ( Humphrey et al., 1996 ).
PY - 2005/12
Y1 - 2005/12
N2 - The nuclear pore complex, through the interaction of its proteins with transport receptors, controls the transport of large molecules into and out of the cell's nucleus. There is ample evidence for proteins with FG sequence repeats playing an essential role in this control. Previous studies have elucidated binding spots for FG sequence repeats on the surface of the transport receptor importin-β by X-ray crystallography and mutational studies. Molecular dynamics simulations have been performed to characterize the interaction of FG sequence repeats with the transport receptor. Observed binding spots have been verified and novel sites discovered, suggesting that importin-β features many more binding spots than suspected so far. The observed binding spots are in accord with several models of nucleocytoplasmic transport, and the large number of binding spots on importin-β may be necessary for the pore complex to distinguish between importin-β and inert proteins, and to allow for its passage through the pore.
AB - The nuclear pore complex, through the interaction of its proteins with transport receptors, controls the transport of large molecules into and out of the cell's nucleus. There is ample evidence for proteins with FG sequence repeats playing an essential role in this control. Previous studies have elucidated binding spots for FG sequence repeats on the surface of the transport receptor importin-β by X-ray crystallography and mutational studies. Molecular dynamics simulations have been performed to characterize the interaction of FG sequence repeats with the transport receptor. Observed binding spots have been verified and novel sites discovered, suggesting that importin-β features many more binding spots than suspected so far. The observed binding spots are in accord with several models of nucleocytoplasmic transport, and the large number of binding spots on importin-β may be necessary for the pore complex to distinguish between importin-β and inert proteins, and to allow for its passage through the pore.
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U2 - 10.1016/j.str.2005.09.007
DO - 10.1016/j.str.2005.09.007
M3 - Article
C2 - 16338415
AN - SCOPUS:28844445505
SN - 0969-2126
VL - 13
SP - 1869
EP - 1879
JO - Structure with Folding & design
JF - Structure with Folding & design
IS - 12
ER -