Abstract
The crystal structure of the NTF2-like domain of the Drosophila homolog of Ras GTPase SH3 Binding Protein (G3BP), Rasputin, was determined at 2.7. å 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.
Original language | English |
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Journal | Biochemical and Biophysical Research Communications |
Volume | 420 |
Issue number | 1 |
Pages (from-to) | 188-92 |
Number of pages | 5 |
ISSN | 0006-291X |
DOIs | |
Publication status | Published - 30 Mar 2012 |
Keywords
- Amino Acid Sequence
- Animals
- Carrier Proteins
- Crystallography, X-Ray
- Drosophila Proteins
- HEPES
- Molecular Sequence Data
- Nucleocytoplasmic Transport Proteins
- Protein Structure, Secondary
- Protein Structure, Tertiary