Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

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

MPG-Autoren
/persons/resource/persons15388

Kühnel,  K.
Research Group of Autophagy, MPI for Biophysical Chemistry, Max Planck Society;

Externe Ressourcen

http://www.pnas.org/content/101/49/17027.full.pdf+html
(Verlagsversion)

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)

1944022.pdf
(Verlagsversion), 606KB

Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Kühnel, K., Jarchau, T., Wolf, E., Schlichting, I., Walter, U., Wittinghofer, A., et al. (2004). 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, 101(49), 17027-17032. doi:10.1073/pnas.0403069101.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0015-8B1E-B
Zusammenfassung
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.