TY - JOUR
T1 - Cse1p-Binding Dynamics Reveal a Binding Pattern for FG-Repeat Nucleoporins on Transport Receptors
AU - Isgro, Timothy A.
AU - Schulten, Klaus
N1 - Funding Information:
The authors acknowledge support from National Institutes of Health grant P41RR05969. K.S. was supported by the Humboldt Foundation. The authors also gladly acknowledge supercomputer time provided by the National Center for Supercomputing Applications and the Pittsburgh Supercomputer Center through the National Science Foundation and the Large Resources Allocation Committee grant MCA93S028. All molecular images in this paper were prepared by using the molecular visualization software VMD ( Humphrey et al., 1996 ).
PY - 2007/8/14
Y1 - 2007/8/14
N2 - Nuclear pore proteins with phenylalanine-glycine repeats are vital to the functional transport of molecules across the nuclear pore complex. The current study investigates the binding of these FG-nucleoporins to the Cse1p:Kap60p:RanGTP nuclear export complex. Fourteen binding spots for FG-nucleoporin peptides are revealed on the surface of Cse1p, and 5 are revealed on the Kap60p surface. Taken together, and along with binding data for two other transport receptors, the data suggest that the ability to bind FG-nucleoporins by itself is not enough to ensure viable nuclear transport. Rather, it is proposed that the density of binding spots on the transport receptor surface is key in determining transport viability. The number of binding spots on the transport receptor surface should be large enough to ensure multiple, simultaneous FG-repeat binding, and their arrangement should be close enough to ensure multiple binding from the same FG-nucleoporin.
AB - Nuclear pore proteins with phenylalanine-glycine repeats are vital to the functional transport of molecules across the nuclear pore complex. The current study investigates the binding of these FG-nucleoporins to the Cse1p:Kap60p:RanGTP nuclear export complex. Fourteen binding spots for FG-nucleoporin peptides are revealed on the surface of Cse1p, and 5 are revealed on the Kap60p surface. Taken together, and along with binding data for two other transport receptors, the data suggest that the ability to bind FG-nucleoporins by itself is not enough to ensure viable nuclear transport. Rather, it is proposed that the density of binding spots on the transport receptor surface is key in determining transport viability. The number of binding spots on the transport receptor surface should be large enough to ensure multiple, simultaneous FG-repeat binding, and their arrangement should be close enough to ensure multiple binding from the same FG-nucleoporin.
KW - CELLBIO
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U2 - 10.1016/j.str.2007.06.011
DO - 10.1016/j.str.2007.06.011
M3 - Article
C2 - 17698002
AN - SCOPUS:34547657392
SN - 0969-2126
VL - 15
SP - 977
EP - 991
JO - Structure
JF - Structure
IS - 8
ER -