2ihs
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Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide
OverviewOverview
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.
About this StructureAbout this Structure
2IHS is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for protein recognition by B30.2/SPRY domains., Woo JS, Suh HY, Park SY, Oh BH, Mol Cell. 2006 Dec 28;24(6):967-76. PMID:17189197
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