The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat
Kühnel, Karin Jarchau, Thomas Wolf, Eva Schlichting, Ilme Walter, Ulrich Wittinghofer, Alfred × Strelkov, Sergei #
Proceedings of the National Academy of Sciences of the United States of America vol:101 issue:49 pages:17027-32
The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-A resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed alpha-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 degrees C.