Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 420, Issue 1, Pages 188-192Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.02.140
Keywords
Rin; Rasputin; G3BP; RasGAP; NTF2; Crystal structure; Ras signaling
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Funding
- Alfred Benzon Foundation
- Brdr. Hartmann Foundation
- Danish Natural Science Council through DANSCATT
- University of Copenhagen
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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 angstrom resolution. The overall structure is highly similar to nuclear transport factor 2: It is a homodimer comprised of a beta-sheet and three alpha-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. (C) 2012 Elsevier Inc. All rights reserved.
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