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

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.
Mesh Terms:
Amino Acid Sequence, Animals, Biopolymers, Cell Adhesion Molecules, Centrifugation, Density Gradient, Circular Dichroism, DNA-Binding Proteins, Dogs, Humans, Hydrogen-Ion Concentration, Mice, Microfilament Proteins, Molecular Sequence Data, Nitrogen Isotopes, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments, Phosphoproteins, Protein Structure, Secondary, Protein Structure, Tertiary, Rats, Sequence Homology, Amino Acid, Temperature, Thermodynamics
Biochemistry
Date: Sep. 17, 2002
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