2fnj

From Proteopedia

Crystal structure of a B30.2/SPRY domain-containing protein GUSTAVUS in complex with Elongin B and Elongin C

Overview

The B30.2/SPRY domain is present in approximately 700 eukaryotic, (approximately 150 human) proteins, including medically important proteins, such as TRIM5alpha and Pyrin. Nonetheless, the functional role of this, modular domain remained unclear. Here, we report the crystal structure of, an SPRY-SOCS box family protein GUSTAVUS in complex with Elongins B and C, revealing a highly distorted two-layered beta-sandwich core structure of, its B30.2/SPRY domain. Ensuing studies identified one end of the, beta-sandwich as the surface interacting with an RNA helicase VASA with a, 40 nM dissociation constant. The sequence variation in TRIM5alpha, responsible for HIV-1 restriction and most of the mutations in Pyrin, causing familial Mediterranean fever map on this surface, implicating the, corresponding region in many B30.2/SPRY domains as the ligand-binding, site. The amino acids lining the binding surface are highly variable among, the B30.2/SPRY domains, suggesting that these domains are, protein-interacting modules, which recognize a specific individual partner, protein rather than a consensus sequence motif.

About this Structure

2FNJ is a Protein complex structure of sequences from Drosophila melanogaster and Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural and functional insights into the B30.2/SPRY domain., Woo JS, Imm JH, Min CK, Kim KJ, Cha SS, Oh BH, EMBO J. 2006 Mar 22;25(6):1353-63. Epub 2006 Feb 23. PMID:16498413

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