The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17027-32. doi: 10.1073/pnas.0403069101. Epub 2004 Nov 29.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Amino Acid Sequence
  • Cell Adhesion Molecules / chemistry*
  • Cell Adhesion Molecules / physiology
  • Crystallography, X-Ray
  • Dimerization
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Microfilament Proteins
  • Molecular Structure
  • Peptide Fragments / chemistry
  • Phosphoproteins / chemistry*
  • Phosphoproteins / physiology
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • Actins
  • Cell Adhesion Molecules
  • Microfilament Proteins
  • Peptide Fragments
  • Phosphoproteins
  • vasodilator-stimulated phosphoprotein

Associated data

  • PDB/1USD
  • PDB/1USE