This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2ihs
From Proteopedia
|
Crystal structure of the B30.2/SPRY domain of GUSTAVUS in complex with a 20-residue VASA peptide
Overview
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 Structure
2IHS is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 12:19:36 2007
