The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.
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ABSTRACT:
SUBMITTER: Kuhnel K
PROVIDER: S-EPMC535362 | biostudies-literature | 2004 Dec
REPOSITORIES: biostudies-literature
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The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.
Kühnel Karin K Jarchau Thomas T Wolf Eva E Schlichting Ilme I Walter Ulrich U Wittinghofer Alfred A Strelkov Sergei V SV
Proceedings of the National Academy of Sciences of the United States of America 20041129 49
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 ...[more]
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