2ihs
Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptideCrystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide
Structural highlights
FunctionGUS_DROME Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedB30.2/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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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