Abstract
The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-Å resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed α-helical coiled-coil structure with a similar degree of supercoiling as found in the widespread left-handed coiled coils with heptad repeats. The basis for the right-handed geometry of VASP TD is a 15-residue repeat in its amino acid sequence, which reveals a characteristic pattern of hydrophobic residues. Hydrophobic interactions and a network of salt bridges render VASP TD highly thermostable with a melting point of 120°C.
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Dates
Type | When |
---|---|
Created | 20 years, 9 months ago (Nov. 29, 2004, 8:25 p.m.) |
Deposited | 3 years, 4 months ago (April 12, 2022, 9:37 a.m.) |
Indexed | 2 days, 19 hours ago (Aug. 31, 2025, 6:24 a.m.) |
Issued | 20 years, 9 months ago (Nov. 29, 2004) |
Published | 20 years, 9 months ago (Nov. 29, 2004) |
Published Online | 20 years, 9 months ago (Nov. 29, 2004) |
Published Print | 20 years, 8 months ago (Dec. 7, 2004) |
@article{K_hnel_2004, title={The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat}, volume={101}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0403069101}, DOI={10.1073/pnas.0403069101}, number={49}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Kühnel, Karin and Jarchau, Thomas and Wolf, Eva and Schlichting, Ilme and Walter, Ulrich and Wittinghofer, Alfred and Strelkov, Sergei V.}, year={2004}, month=nov, pages={17027–17032} }