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

AUTOR(ES)

Kühnel, Karin

FONTE

National Academy of Sciences

RESUMO

The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-Å resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed α-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°C.

Documentos Relacionados

• DYSPHASIA FOLLOWING RIGHT TEMPORAL LOBECTOMY IN A RIGHT-HANDED MAN
• The conducting form of gramicidin A is a right-handed double-stranded double helix
• THE OPTICAL ROTATORY DISPERSION OF RIGHT-HANDED α-HELICES IN SPERM WHALE MYOGLOBIN*
• Origin of the right-handed twist of beta-sheets of poly(LVal) chains.
• Rhizobium meliloti swims by unidirectional, intermittent rotation of right-handed flagellar helices.