Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein

MPG-Autoren
/persons/resource/persons117899

Stier,  Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95148

Scheffzek,  Klaus
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

http://journals.iucr.org/d/issues/2004/12/02/bw5061/bw5061.pdf
(beliebiger Volltext)

https://doi.org/10.1107/S0907444904026861
(beliebiger Volltext)

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Bonneau, F., D Angelo, I., Welti, S., Stier, G., Ylänne, J., & Scheffzek, K. (2004). Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein. Acta Crystallographica Section D-Biological Crystallography, 60(2), 2364-2367. doi:10.1107/S0907444904026861.


Zitierlink: https://hdl.handle.net/21.11116/0000-0001-E809-0
Zusammenfassung
Neurofibromin (MW 320 kDa) is the protein responsible for the pathogenesis of neurofibromatosis type 1 (NF1), one of the most common genetic diseases worldwide. The neurofibromin GAP-related domain (GRD, MW 38 kDa) possess a Ras-specific GTPase-activating protein property, which is at present its only clear biochemical function. This article describes the study of the bacterial production and preliminary X-ray crystallographic analysis of a neurofibromin fragment located at the C-terminal end of the GRD, which contains a region reported to be homologous to the yeast Sec14p lipid exchange protein. Of the three crystal variants obtained, a tetragonal form diffracted to a resolution of at least 2.3 A.