2IHS

Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide

Summary for 2IHS

• Entry DOI: 10.2210/pdb2ihs/pdb
• Related: 2FBE 2FNJ
• Descriptor: CG2944-PF, isoform F, 20-mer from ATP-dependent RNA helicase vasa (3 entities in total)
• Functional Keywords: b30.2/spry, gustavus, vasa, spry-containing socs box, f-box-spry, trim family, peptide binding protein
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Cytoplasm: P09052
• Total number of polymer chains: 4
• Total formula weight: 53356.64

Authors

Woo, J.S.,Park, S.Y.,Oh, B.H. (deposition date: 2006-09-27, release date: 2007-01-16, Last modification date: 2024-10-16)

Primary citation

Woo, J.S.,Suh, H.Y.,Park, S.Y.,Oh, B.H.
Structural Basis for Protein Recognition by B30.2/SPRY Domains
Mol.Cell, 24:967-976, 2006

PubMed Abstract: B30.2/SPRY domains are found in numerous proteins that cover a wide spectrum of biological functions, including regulation of cytokine signaling and innate retroviral restriction. Herein, we report the crystal structure of the B30.2/SPRY domain of a SPRY domain-containing SOCS box (SSB) protein, GUSTAVUS, complexed with a 20 amino acid peptide derived from the RNA helicase VASA, revealing how these domains recognize target proteins. The peptide-binding site is conformationally rigid and has a preformed pocket. The interaction between the pocket and the Asp-Ile-Asn-Asn-Asn-Asn sequence within the peptide accounts for the high-affinity binding between GUSTAVUS and VASA. This observation led to a facile identification of the Glu-Leu-Asn-Asn-Asn-Leu sequence as the recognition motif in a proapoptotic protein Par-4 for its interaction with a GUSTAVUS homolog, SSB-1. Ensuing analyses indicated that many B30.2/SPRY domains have a similar preformed pocket, which would allow them to bind multiple targets.

PubMed: 17189197
DOI: 10.1016/j.molcel.2006.11.009

Experimental method

X-RAY DIFFRACTION (2.2 Å)