FinGering the Merchandise

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Science  06 Jan 2006:
Vol. 311, Issue 5757, pp. 17
DOI: 10.1126/science.311.5757.17a

Remarkable advances in the application of physical methods to biological systems have yielded a bumper crop of achievements taken to the nth degree, such as atomic-resolution models of enormously complicated macromolecular assemblies and real-time tracking of single molecules within live cells. It is, however, not yet feasible to do both at once, which would allow for the spatiotemporal visualization of protein-protein interactions at the scale of individual amino acid residues, and current approaches have relied on bioinformatics and laborious experimental trials.

Molecular dynamics simulations provide a way to look at these events, and Isgro and Schulten confirm previous results and uncover new ones in their analysis of the nuclear transport factor β-importin and phenylalanineglycine (FG) repeat-containing peptides; the latter are stand-ins for the nucleoporins, components of the nuclear pore complex that mediates the passage of large molecules (10 to 40 nm in diameter) across the nuclear membrane. FG binding sites on transport factors have been identified in structural and biochemical studies, and proposals for how the nucleoporins gate entry into the nucleus are based on multiple semi-strong sites (1 to 100 nM affinity) that turn the pore into an examination room where import cargoes can be palpated and then accepted or rejected. — GJC

Structure 13, 1869 (2005).

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