The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat
Proceedings of the National Academy of Sciences of the United States of America. Bd. 101. H. 49. Washington, DC: National Acad. of Sciences 2004 S. 17027 - 17032
Erscheinungsjahr: 2004
ISBN/ISSN: 0027-8424
Publikationstyp: Zeitschriftenaufsatz
Sprache: Englisch
Doi/URN: 10.1073/pnas.0403069101
| Geprüft: | Bibliothek |
Inhaltszusammenfassung
The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-Angstrom resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed a-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,...The vasodilator-stimulated phosphoprotein (VASP) is a key regulator of actin dynamics. We have determined the 1.3-Angstrom resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP. This domain forms a right-handed a-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 120degreesC.» weiterlesen» einklappen
Autoren
Klassifikation
DFG Fachgebiet:
2.12 - Pflanzenwissenschaften
DDC Sachgruppe:
Pflanzen (Botanik)
