Relaxation, equilibrium oligomerization, and molecular symmetry of the VASP (336-380) EVH2 tetramer

Biochemistry. 2002 Sep 17;41(37):11143-51. doi: 10.1021/bi020379x.


An investigation of the structural and dynamic properties of the C-terminal fragment of the human protein VASP (VASP 336-380) has been performed. Full length VASP has been shown to be tetrameric in solution, and the C-terminal 45 residues of the protein have been suggested to be responsible for the oligomerization. We have expressed and purified a C-terminal fragment of the human VASP protein from residue 336-380. It was found to form a stable domain in its own right. The fragment was shown by CD spectroscopy to form a helical structure, stable under a wide range of temperature and pH conditions. A (15)N-HSQC-experiment exhibits only one set of peaks, suggesting a high degree of symmetry for a putative oligomer. Measurements of the rotational correlation time tau(C) of the molecule and analytical ultracentrifugation data show VASP (336-380) to be entirely tetrameric in solution. The secondary structure was confirmed from a (15)N-NOESY-HSQC experiment and is completely alpha-helical. We conclude that VASP (336-380) forms a tetramer in solution via a coiled coil arrangement and is solely responsible for tetramerization of full-length VASP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biopolymers / chemistry
  • Cell Adhesion Molecules / chemistry*
  • Centrifugation, Density Gradient
  • Circular Dichroism
  • DNA-Binding Proteins / chemistry*
  • Dogs
  • Humans
  • Hydrogen-Ion Concentration
  • Mice
  • Microfilament Proteins
  • Molecular Sequence Data
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Peptide Fragments / chemistry*
  • Phosphoproteins / chemistry*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Rats
  • Sequence Homology, Amino Acid*
  • Temperature
  • Thermodynamics


  • Biopolymers
  • Cell Adhesion Molecules
  • DNA-Binding Proteins
  • ENA-VASP proteins
  • Microfilament Proteins
  • Nitrogen Isotopes
  • Peptide Fragments
  • Phosphoproteins
  • vasodilator-stimulated phosphoprotein