The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat.
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.
Kühnel
Karin
K
Max-Planck-Institut für Molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Jarchau
Thomas
T
Wolf
Eva
E
Schlichting
Ilme
I
Walter
Ulrich
U
Wittinghofer
Alfred
A
Strelkov
Sergei V
SV
D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000502:physiology; D018360:Crystallography, X-Ray; D019281:Dimerization; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008840:Microfilament Proteins; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry; D010750:Phosphoproteins / Q000737:chemistry* / Q000502:physiology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D000098662:Vasodilator-Stimulated Phosphoprotein
D000199:Actins; D015815:Cell Adhesion Molecules; D008840:Microfilament Proteins; D010446:Peptide Fragments; D010750:Phosphoproteins; D000098662:Vasodilator-Stimulated Phosphoprotein