Structural and functional insights into the B30.2/SPRY domain

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The B30.2/SPRY domain is present in similar to 700 eukaryotic (similar to 150 human) proteins, including medically important proteins such as TRIM5 alpha 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 TRIM5 alpha 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.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2006-03
Language
English
Article Type
Article
Keywords

FAMILIAL MEDITERRANEAN FEVER; RETROVIRAL RESTRICTION; SOCS-BOX; CARBOHYDRATE-RECOGNITION; STRUCTURE PREDICTION; INTERACTING PROTEIN; CRYSTAL-STRUCTURE; SPRY-DOMAIN; OLD-WORLD; TRIM5-ALPHA

Citation

EMBO JOURNAL, v.25, no.6, pp.1353 - 1363

ISSN
0261-4189
DOI
10.1038/sj.emboj.7600994
URI
http://hdl.handle.net/10203/92871
Appears in Collection
BS-Journal Papers(저널논문)
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