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Monomeric and dimeric conformation of the vinculin tail five-helix bundle in solution studied by EPR spectroscopy. | LitMetric

AI Article Synopsis

  • - The protein vinculin is essential for cell adhesion and movement, connecting the actin cytoskeleton to adhesion sites.
  • - Researchers studied the structure of the vinculin tail dimer using advanced techniques to understand its function better, confirming that its shape remains stable in solution.
  • - They found that when vinculin interacts with F-actin, there is a significant increase in distance between certain parts of the protein, indicating a change upon binding.

Article Abstract

The cytoskeletal adaptor protein vinculin plays an important role in the control of cell adhesion and migration, linking the actin cytoskeleton to adhesion receptor complexes in cell adhesion sites. The conformation of the vinculin tail dimer, which is crucial for protein function, was analyzed using site-directed spin labeling in electron paramagnetic resonance spectroscopy. Interspin distances for a set of six singly and four doubly spin-labeled mutants of the tail domain of vinculin were determined and used as constraints for modeling of the vinculin tail dimer. A comparison of the results obtained by molecular dynamic simulations and a rotamer library approach reveals that the crystal structure of the vinculin tail monomer is essentially preserved in aqueous solution. The orientation of monomers within the dimer observed previously by x-ray crystallography agrees with the solution electron paramagnetic resonance data. Furthermore, the distance between positions 1033 is shown to increase by >3 nm upon interaction of the vinculin tail domain with F-actin.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3183806PMC
http://dx.doi.org/10.1016/j.bpj.2011.08.048DOI Listing

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