title: Crystal structure of the Rasputin NTF2-like domain from Drosophila melanogaster.
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.
authors.affiliation: Biostructural Research, Department of Drug Design and Pharmacology, Faculty of Health Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark. tv@farma.ku.dk
authors.forename: Tina
authors.initials: T
authors.lastname: Vognsen
authors.forename: Ole
authors.initials: O
authors.lastname: Kristensen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry* / Q000235:genetics; D006531:HEPES / Q000737:chemistry; D008969:Molecular Sequence Data; D029543:Nucleocytoplasmic Transport Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D002352:Carrier Proteins; D029721:Drosophila Proteins; C503609:Ntf-2 protein, Drosophila; D029543:Nucleocytoplasmic Transport Proteins; C492054:rin protein, Drosophila; D006531:HEPES