Skip to Content
Merck
  • Crystal structure of the Rasputin NTF2-like domain from Drosophila melanogaster.

Crystal structure of the Rasputin NTF2-like domain from Drosophila melanogaster.

Biochemical and biophysical research communications (2012-03-15)
Tina Vognsen, Ole Kristensen
ABSTRACT

The crystal structure of the NTF2-like domain of the Drosophila homolog of Ras GTPase SH3 Binding Protein (G3BP), Rasputin, was determined at 2.7Å resolution. The overall structure is highly similar to nuclear transport factor 2: It is a homodimer comprised of a β-sheet and three α-helices forming a cone-like shape. However, known binding sites for RanGDP and FxFG containing peptides show electrostatic and steric differences compared to nuclear transport factor 2. A HEPES molecule bound in the structure suggests a new, and possibly physiologically relevant, ligand binding site.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
HEPES sodium salt, ≥99.5% (titration), free-flowing, Redi-Dri
Sigma-Aldrich
HEPES, BioUltra, for molecular biology, ≥99.5% (T)
Sigma-Aldrich
HEPES, ≥99.5% (titration)
Sigma-Aldrich
HEPES, BioPerformance Certified, ≥99.5% (titration), suitable for cell culture
Sigma-Aldrich
HEPES, BioXtra, suitable for mouse embryo cell culture, ≥99.5% (titration)
SAFC
HEPES
SAFC
HEPES sodium salt
Sigma-Aldrich
HEPES, BioXtra, pH 5.0-6.5 (1 M in H2O), ≥99.5% (titration)
Sigma-Aldrich
HEPES sodium salt solution, BioReagent, 1M, suitable for cell culture
Sigma-Aldrich
HEPES sodium salt, BioPerformance Certified, suitable for cell culture, ≥99.0%
Sigma-Aldrich
HEPES sodium salt, ≥99.0% (titration)
Sigma-Aldrich
HEPES solution, 1 M, pH 7.0-7.6, sterile-filtered, BioReagent, suitable for cell culture
Sigma-Aldrich
HEPES buffer solution, 1 M in H2O
Sigma-Aldrich
HEPES solution, BioPerformance Certified, 1 M, suitable for cell culture, 0.2 μm filtered